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  • Protein Structure, Tertiary  (54)
  • American Association for the Advancement of Science (AAAS)  (54)
  • Annual Reviews
  • Blackwell Publishing Ltd
  • 2005-2009  (54)
  • 1980-1984
  • 1930-1934
  • 2005  (54)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (54)
  • Annual Reviews
  • Blackwell Publishing Ltd
Years
  • 2005-2009  (54)
  • 1980-1984
  • 1930-1934
Year
  • 1
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    Cell signaling. Frizzled at the cutting edge of the synapse (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez Arias, Alfonso -- New York, N.Y. -- Science. 2005 Nov 25;310(5752):1284-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK. ama11@hermes.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16311322" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Cell Nucleus/metabolism ; Drosophila Proteins/chemistry/*metabolism ; Drosophila melanogaster/genetics/*metabolism ; Endocytosis ; Frizzled Receptors ; Models, Neurological ; Mutation ; Neuromuscular Junction/*metabolism ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/*metabolism ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter/chemistry/*metabolism ; *Signal Transduction ; Wnt1 Protein
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Micropylar pollen tube guidance by egg apparatus 1 of maize (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-01
    Description: Pollen tube guidance precedes the double fertilization of flowering plants. Here, we report the identification of a small maize protein of 94 amino acids involved in short-range signaling required for pollen tube attraction by the female gametophyte. ZmEA1 is exclusively expressed in the egg apparatus, consisting of the egg cell and two synergids. Chimeric ZmEA1 fused to green fluorescent protein (ZmEA1:GFP) was first visible within the filiform apparatus and later was localized to nucellar cell walls below the micropylar opening of the ovule. Transgenic down-regulation of the ZmEA1 gene led to ovule sterility caused by loss of close-range pollen tube guidance to the micropyle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marton, Mihaela L -- Cordts, Simone -- Broadhvest, Jean -- Dresselhaus, Thomas -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biocenter Klein Flottbek, Developmental Biology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, D-22609 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antisense Elements (Genetics) ; Crosses, Genetic ; DNA, Complementary ; Flowers/growth & development/*physiology ; Genes, Plant ; Green Fluorescent Proteins/metabolism ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/*physiology ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Reproduction ; Seeds/physiology ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Zea mays/*genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-17
    Description: Translesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of poleta and poliota to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of poleta is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bienko, Marzena -- Green, Catherine M -- Crosetto, Nicola -- Rudolf, Fabian -- Zapart, Grzegorz -- Coull, Barry -- Kannouche, Patricia -- Wider, Gerhard -- Peter, Matthias -- Lehmann, Alan R -- Hofmann, Kay -- Dikic, Ivan -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1821-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biochemistry II, Goethe University Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Line ; Computational Biology ; DNA/*biosynthesis ; *DNA Damage ; DNA Repair ; DNA Replication ; DNA-Directed DNA Polymerase/*chemistry/genetics/*metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Point Mutation ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Binding ; Protein Conformation ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Transfection ; Ubiquitin/*metabolism ; Xeroderma Pigmentosum/genetics ; Zinc Fingers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Toward high-resolution de novo structure prediction for small proteins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-17
    Description: The prediction of protein structure from amino acid sequence is a grand challenge of computational molecular biology. By using a combination of improved low- and high-resolution conformational sampling methods, improved atomically detailed potential functions that capture the jigsaw puzzle-like packing of protein cores, and high-performance computing, high-resolution structure prediction (〈1.5 angstroms) can be achieved for small protein domains (〈85 residues). The primary bottleneck to consistent high-resolution prediction appears to be conformational sampling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradley, Philip -- Misura, Kira M S -- Baker, David -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Washington, Department of Biochemistry, and Howard Hughes Medical Institute, Box 357350, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemistry, Physical ; *Computational Biology ; Computer Simulation ; Hydrogen Bonding ; Models, Molecular ; Monte Carlo Method ; Physicochemical Phenomena ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry ; Sequence Alignment ; Thermodynamics
    Print ISSN: 0036-8075
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  • 5
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    Structural biology. Flipping lipids: is the third time the charm? (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davidson, Amy L -- Chen, Jue -- New York, N.Y. -- Science. 2005 May 13;308(5724):963-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA. davidson@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890866" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/*metabolism ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Bacterial Proteins/*chemistry/*metabolism ; Cell Membrane/*chemistry ; Crystallography, X-Ray ; Dimerization ; Electron Spin Resonance Spectroscopy ; Escherichia coli/chemistry ; Escherichia coli Proteins/chemistry/metabolism ; Hydrolysis ; Lipid A/metabolism ; Lipid Bilayers ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Salmonella typhimurium/*chemistry ; Spin Labels ; Vanadates/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Crystal structure of the malaria vaccine candidate apical membrane antigen 1 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-26
    Description: Apical membrane antigen 1 from Plasmodium is a leading malaria vaccine candidate. The protein is essential for host-cell invasion, but its molecular function is unknown. The crystal structure of the three domains comprising the ectoplasmic region of the antigen from P. vivax, solved at 1.8 angstrom resolution, shows that domains I and II belong to the PAN motif, which defines a superfamily of protein folds implicated in receptor binding. We also mapped the epitope of an invasion-inhibitory monoclonal antibody specific for the P. falciparum ortholog and modeled this to the structure. The location of the epitope and current knowledge on structure-function correlations for PAN domains together suggest a receptor-binding role during invasion in which domain II plays a critical part. These results are likely to aid vaccine and drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizarro, Juan Carlos -- Vulliez-Le Normand, Brigitte -- Chesne-Seck, Marie-Laure -- Collins, Christine R -- Withers-Martinez, Chrislaine -- Hackett, Fiona -- Blackman, Michael J -- Faber, Bart W -- Remarque, Edmond J -- Kocken, Clemens H M -- Thomas, Alan W -- Bentley, Graham A -- MC_U117532063/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):408-11. Epub 2005 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite d'Immunologie Structurale, Centre National de la Recherche Scientifique, URA 2185, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731407" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Protozoan/*chemistry/immunology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Epitope Mapping ; Epitopes ; Heparin/metabolism ; Malaria Vaccines ; Membrane Proteins/*chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Plasmodium falciparum/chemistry/immunology ; Plasmodium vivax/chemistry/*immunology ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protozoan Proteins/*chemistry/immunology ; Recombinant Proteins/chemistry ; Sequence Alignment
    Print ISSN: 0036-8075
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  • 7
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    Nodulation signaling in legumes requires NSP2, a member of the GRAS family of transcriptional regulators (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-18
    Description: Rhizobial bacteria enter a symbiotic interaction with legumes, activating diverse responses in roots through the lipochito oligosaccharide signaling molecule Nod factor. Here, we show that NSP2 from Medicago truncatula encodes a GRAS protein essential for Nod-factor signaling. NSP2 functions downstream of Nod-factor-induced calcium spiking and a calcium/calmodulin-dependent protein kinase. We show that NSP2-GFP expressed from a constitutive promoter is localized to the endoplasmic reticulum/nuclear envelope and relocalizes to the nucleus after Nod-factor elicitation. This work provides evidence that a GRAS protein transduces calcium signals in plants and provides a possible regulator of Nod-factor-inducible gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kalo, Peter -- Gleason, Cynthia -- Edwards, Anne -- Marsh, John -- Mitra, Raka M -- Hirsch, Sibylle -- Jakab, Julia -- Sims, Sarah -- Long, Sharon R -- Rogers, Jane -- Kiss, Gyorgy B -- Downie, J Allan -- Oldroyd, Giles E D -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1786-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Disease and Stress Biology and Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961668" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Calcium/metabolism ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/metabolism ; Cell Nucleus/metabolism ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; Lipopolysaccharides/*metabolism ; Medicago/genetics/*metabolism/*microbiology ; Molecular Sequence Data ; Mutation ; Oligonucleotide Array Sequence Analysis ; Peas/genetics/metabolism ; Plant Proteins/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Sinorhizobium meliloti/*physiology ; Symbiosis ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 8
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    Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: Chlorinated natural products include vancomycin and cryptophycin A. Their biosynthesis involves regioselective chlorination by flavin-dependent halogenases. We report the structural characterization of tryptophan 7-halogenase (PrnA), which regioselectively chlorinates tryptophan. Tryptophan and flavin adenine dinucleotide (FAD) are separated by a 10 angstrom-long tunnel and bound by distinct enzyme modules. The FAD module is conserved in halogenases and is related to flavin-dependent monooxygenases. On the basis of biochemical studies, crystal structures, and by analogy with monooxygenases, we predict that FADH2 reacts with O2 to make peroxyflavin, which is decomposed by Cl-. The resulting HOCl is guided through the tunnel to tryptophan, where it is activated to participate in electrophilic aromatic substitution.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315827/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315827/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, Changjiang -- Flecks, Silvana -- Unversucht, Susanne -- Haupt, Caroline -- van Pee, Karl-Heinz -- Naismith, James H -- BB/C000080/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BBS/B/14426/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2216-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Biomolecular Sciences, EaStchem, University of St. Andrews, St. Andrews KY16 9ST, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195462" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Chlorides/*metabolism ; Crystallography, X-Ray ; Dimerization ; Flavin-Adenine Dinucleotide/analogs & derivatives/metabolism ; Hydrogen Bonding ; Hypochlorous Acid/metabolism ; Indoles/metabolism ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/*chemistry/isolation & purification/metabolism ; Oxygen/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pseudomonas fluorescens/*enzymology ; Tryptophan/analogs & derivatives/metabolism
    Print ISSN: 0036-8075
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  • 9
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    Structure of SARS coronavirus spike receptor-binding domain complexed with receptor (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-17
    Description: The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Fang -- Li, Wenhui -- Farzan, Michael -- Harrison, Stephen C -- AI061601/AI/NIAID NIH HHS/ -- CA13202/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1864-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166518" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antibodies, Viral/immunology ; Binding Sites ; Carboxypeptidases/*chemistry/metabolism ; Cell Line ; Crystallography, X-Ray ; Disease Outbreaks ; Epitopes ; Glycosylation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/*chemistry/genetics/immunology/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Peptidyl-Dipeptidase A ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*chemistry/metabolism ; SARS Virus/*chemistry/genetics/physiology ; Severe Acute Respiratory Syndrome/transmission/*virology ; Species Specificity ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/*chemistry/genetics/immunology/*metabolism ; Viral Vaccines ; Viverridae/virology
    Print ISSN: 0036-8075
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  • 10
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    Structural insights into the activity of enhancer-binding proteins (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: Activators of bacterial sigma54-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic electron microscopy (cryo-EM) a 20 angstrom resolution structure of an activator, phage shock protein F [PspF(1-275)], which is bound to an ATP transition state analog in complex with its basal factor, sigma54. By fitting the crystal structure of PspF(1-275) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma54. Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma54.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2756573/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2756573/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rappas, Mathieu -- Schumacher, Jorg -- Beuron, Fabienne -- Niwa, Hajime -- Bordes, Patricia -- Wigneshweraraj, Sivaramesh -- Keetch, Catherine A -- Robinson, Carol V -- Buck, Martin -- Zhang, Xiaodong -- B17129/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1972-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Imperial College London, London, SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790859" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Cryoelectron Microscopy ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/metabolism ; DNA-Directed RNA Polymerases/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; PII Nitrogen Regulatory Proteins ; *Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Polymerase Sigma 54 ; Sigma Factor/chemistry/metabolism ; Trans-Activators/*chemistry/*metabolism ; Transcription Factors/chemistry/metabolism
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  • 11
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    Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of control-topological, conformational, and covalent-until its release from the membrane is triggered by the P1 holin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, Min -- Arulandu, Arockiasamy -- Struck, Douglas K -- Swanson, Stephanie -- Sacchettini, James C -- Young, Ry -- GM27099/GM/NIGMS NIH HHS/ -- GM62410/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):113-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637279" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage P1/*enzymology ; Binding Sites ; Catalytic Domain ; Cell Membrane/enzymology ; Chemistry, Physical ; Crystallography, X-Ray ; Cysteine/chemistry ; Enzyme Activation ; Escherichia coli/enzymology/virology ; Isomerism ; Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Muramidase/*chemistry/genetics/*metabolism ; Mutation ; Physicochemical Phenomena ; Protein Conformation ; Protein Sorting Signals ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism
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  • 12
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    Cancer. An anchor for tumor cell invasion (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuspa, Stuart H -- Epstein, Ervin H Jr -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1727-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. sy12j@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774745" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma, Squamous Cell/etiology/genetics/pathology/*physiopathology ; Cell Adhesion Molecules/metabolism ; Cell Transformation, Neoplastic ; Collagen Type VII/chemistry/*genetics/*physiology ; Disease Susceptibility ; Epidermolysis Bullosa Dystrophica/complications/*genetics/metabolism/pathology ; Genes, ras ; Humans ; I-kappa B Proteins/genetics/metabolism ; Keratinocytes/*metabolism/pathology ; Mice ; Mutation ; Neoplasm Invasiveness ; Protein Structure, Tertiary ; Skin Neoplasms/etiology/genetics/pathology/*physiopathology ; Transduction, Genetic ; Transforming Growth Factor beta/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    Crystal structure of human toll-like receptor 3 (TLR3) ectodomain (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-18
    Description: Toll-like receptors (TLRs) play key roles in activating immune responses during infection. The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs). Asparagines conserved in the 24-residue LRR motif contribute extensive hydrogen-bonding networks for solenoid stabilization. TLR3 is largely masked by carbohydrate, but one face is glycosylation-free, which suggests its potential role in ligand binding and oligomerization. Highly conserved surface residues and a TLR3-specific LRR insertion form a homodimer interface in the crystal, whereas two patches of positively charged residues and a second insertion would provide an appropriate binding site for double-stranded RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choe, Jungwoo -- Kelker, Matthew S -- Wilson, Ian A -- AI-42266/AI/NIAID NIH HHS/ -- CA-58896/CA/NCI NIH HHS/ -- T32 AI077606/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):581-5. Epub 2005 Jun 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute (TSRI), 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961631" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; Glycosylation ; Humans ; Hydrogen Bonding ; Leucine/chemistry ; Ligands ; Membrane Glycoproteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Double-Stranded/metabolism ; Receptors, Cell Surface/*chemistry/metabolism ; Repetitive Sequences, Amino Acid ; Signal Transduction ; Static Electricity ; Surface Properties ; Toll-Like Receptor 3 ; Toll-Like Receptors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
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    TAZ, a transcriptional modulator of mesenchymal stem cell differentiation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-16
    Description: Mesenchymal stem cells (MSCs) are a pluripotent cell type that can differentiate into several distinct lineages. Two key transcription factors, Runx2 and peroxisome proliferator-activated receptor gamma (PPARgamma), drive MSCs to differentiate into either osteoblasts or adipocytes, respectively. How these two transcription factors are regulated in order to specify these alternate cell fates remains a pivotal question. Here we report that a 14-3-3-binding protein, TAZ (transcriptional coactivator with PDZ-binding motif), coactivates Runx2-dependent gene transcription while repressing PPARgamma-dependent gene transcription. By modulating TAZ expression in model cell lines, mouse embryonic fibroblasts, and primary MSCs in culture and in zebrafish in vivo, we observed alterations in osteogenic versus adipogenic potential. These results indicate that TAZ functions as a molecular rheostat that modulates MSC differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hong, Jeong-Ho -- Hwang, Eun Sook -- McManus, Michael T -- Amsterdam, Adam -- Tian, Yu -- Kalmukova, Ralitsa -- Mueller, Elisabetta -- Benjamin, Thomas -- Spiegelman, Bruce M -- Sharp, Phillip A -- Hopkins, Nancy -- Yaffe, Michael B -- CA042063/CA/NCI NIH HHS/ -- GM60594/GM/NIGMS NIH HHS/ -- GM68762/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1074-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research, Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, E18-580, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099986" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/*cytology ; Animals ; Bone Morphogenetic Protein 2 ; Bone Morphogenetic Proteins/pharmacology ; Cell Differentiation ; Cell Line ; Core Binding Factor Alpha 1 Subunit ; Gene Expression Regulation, Developmental ; Humans ; Mesenchymal Stromal Cells/*cytology/physiology ; Mice ; Neoplasm Proteins/metabolism ; Oligonucleotides, Antisense ; Osteoblasts/*cytology ; Osteocalcin/genetics ; Osteogenesis ; PPAR gamma/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Proteins/chemistry/genetics/*physiology ; RNA, Small Interfering ; Transcription Factors/chemistry/genetics/metabolism/*physiology ; Transcriptional Activation ; Transfection ; Transforming Growth Factor beta/pharmacology ; Zebrafish ; Zebrafish Proteins/genetics/physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Functional genomic analysis of RNA interference in C. elegans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-26
    Description: RNA interference (RNAi) of target genes is triggered by double-stranded RNAs (dsRNAs) processed by conserved nucleases and accessory factors. To identify the genetic components required for RNAi, we performed a genome-wide screen using an engineered RNAi sensor strain of Caenorhabditis elegans. The RNAi screen identified 90 genes. These included Piwi/PAZ proteins, DEAH helicases, RNA binding/processing factors, chromatin-associated factors, DNA recombination proteins, nuclear import/export factors, and 11 known components of the RNAi machinery. We demonstrate that some of these genes are also required for germline and somatic transgene silencing. Moreover, the physical interactions among these potential RNAi factors suggest links to other RNA-dependent gene regulatory pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, John K -- Gabel, Harrison W -- Kamath, Ravi S -- Tewari, Muneesh -- Pasquinelli, Amy -- Rual, Jean-Francois -- Kennedy, Scott -- Dybbs, Michael -- Bertin, Nicolas -- Kaplan, Joshua M -- Vidal, Marc -- Ruvkun, Gary -- GM44619/GM/NIGMS NIH HHS/ -- K08-AG21613/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2005 May 20;308(5725):1164-7. Epub 2005 Mar 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790806" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Caenorhabditis elegans/*genetics/metabolism ; Caenorhabditis elegans Proteins/chemistry/*genetics/metabolism ; Gene Library ; Gene Silencing ; *Genes, Helminth ; *Genome ; Genomics ; Protein Interaction Mapping ; Protein Structure, Tertiary ; *RNA Interference ; RNA Precursors/metabolism ; RNA, Double-Stranded/genetics ; RNA, Helminth/genetics ; Transgenes
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-02
    Description: The existence of specialized molecular chaperones that interact directly with ribosomes is well established in microorganisms. Such proteins bind polypeptides exiting the ribosomal tunnel and provide a physical link between translation and protein folding. We report that ribosome-associated molecular chaperones have been maintained throughout eukaryotic evolution, as illustrated by Mpp11, the human ortholog of the yeast ribosome-associated J protein Zuo. When expressed in yeast, Mpp11 partially substituted for Zuo by partnering with the multipurpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multifunctional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hundley, Heather A -- Walter, William -- Bairstow, Shawn -- Craig, Elizabeth A -- R01GM031107/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 13;308(5724):1032-4. Epub 2005 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802566" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Substitution ; Binding Sites ; Cell Line ; DNA-Binding Proteins/chemistry/*metabolism ; HSC70 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/chemistry/*metabolism ; Oncogene Proteins/chemistry/*metabolism ; Potassium Chloride/pharmacology ; Protein Structure, Tertiary ; Ribosomes/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    T helper cell fate specified by kinase-mediated interaction of T-bet with GATA-3 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-22
    Description: Cell lineage specification depends on both gene activation and gene silencing, and in the differentiation of T helper progenitors to Th1 or Th2 effector cells, this requires the action of two opposing transcription factors, T-bet and GATA-3. T-bet is essential for the development of Th1 cells, and GATA-3 performs an equivalent role in Th2 development. We report that T-bet represses Th2 lineage commitment through tyrosine kinase-mediated interaction between the two transcription factors that interferes with the binding of GATA-3 to its target DNA. These results provide a novel function for tyrosine phosphorylation of a transcription factor in specifying alternate fates of a common progenitor cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, Eun Sook -- Szabo, Susanne J -- Schwartzberg, Pamela L -- Glimcher, Laurie H -- AI48126/AI/NIAID NIH HHS/ -- AI56296/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Lineage ; Cytokines/pharmacology/physiology ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; GATA3 Transcription Factor ; Interleukin-5/genetics ; Mice ; Mice, Inbred BALB C ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/metabolism ; T-Box Domain Proteins ; T-Lymphocytes, Helper-Inducer/cytology/*physiology ; Th1 Cells/cytology/physiology ; Th2 Cells/cytology/*physiology ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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  • 18
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    Type VII collagen is required for Ras-driven human epidermal tumorigenesis (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: Type VII collagen defects cause recessive dystrophic epidermolysis bullosa (RDEB), a blistering skin disorder often accompanied by epidermal cancers. To study the role of collagen VII in these cancers, we examined Ras-driven tumorigenesis in RDEB keratinocytes. Cells devoid of collagen VII did not form tumors in mice, whereas those retaining a specific collagen VII fragment (the amino-terminal noncollagenous domain NC1) were tumorigenic. Forced NC1 expression restored tumorigenicity to collagen VII-null epidermis in a non-cell-autonomous fashion. Fibronectin-like sequences within NC1 (FNC1) promoted tumor cell invasion in a laminin 5-dependent manner and were required for tumorigenesis. Tumor-stroma interactions mediated by collagen VII thus promote neoplasia, and retention of NC1 sequences in a subset of RDEB patients may contribute to their increased susceptibility to squamous cell carcinoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ortiz-Urda, Susana -- Garcia, John -- Green, Cheryl L -- Chen, Lei -- Lin, Qun -- Veitch, Dallas P -- Sakai, Lynn Y -- Lee, Hyangkyu -- Marinkovich, M Peter -- Khavari, Paul A -- AR43799/AR/NIAMS NIH HHS/ -- AR44012/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1773-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉VA Palo Alto Healthcare System, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774758" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Animals ; Antibodies/immunology ; Apoptosis ; Carcinoma, Squamous Cell/etiology/*physiopathology ; Cell Adhesion Molecules/immunology/metabolism ; Cell Proliferation ; Cell Transformation, Neoplastic ; Child ; Collagen Type VII/chemistry/*genetics/immunology/*physiology ; Disease Susceptibility ; Epidermolysis Bullosa Dystrophica/complications/*genetics/metabolism/pathology ; Female ; *Genes, ras ; Humans ; I-kappa B Proteins/genetics/metabolism ; Keratinocytes/*metabolism/pathology ; Male ; Mice ; Mice, SCID ; Middle Aged ; Mutation ; Neoplasm Invasiveness ; Protein Structure, Tertiary ; Skin Neoplasms/etiology/pathology/*physiopathology
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  • 19
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    The pseudo-response regulator Ppd-H1 provides adaptation to photoperiod in barley (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-15
    Description: Plants commonly use photoperiod (day length) to control the timing of flowering during the year, and variation in photoperiod response has been selected in many crops to provide adaptation to different environments and farming practices. Positional cloning identified Ppd-H1, the major determinant of barley photoperiod response, as a pseudo-response regulator, a class of genes involved in circadian clock function. Reduced photoperiod responsiveness of the ppd-H1 mutant, which is highly advantageous in spring-sown varieties, is explained by altered circadian expression of the photoperiod pathway gene CONSTANS and reduced expression of its downstream target, FT, a key regulator of flowering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turner, Adrian -- Beales, James -- Faure, Sebastien -- Dunford, Roy P -- Laurie, David A -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):1031-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crop Genetics Department, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284181" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Circadian Rhythm ; Cloning, Molecular ; Crosses, Genetic ; Flowers/physiology ; Gene Expression Profiling ; Gene Expression Regulation, Plant ; *Genes, Plant ; Hordeum/genetics/*physiology ; Molecular Sequence Data ; Mutation ; *Photoperiod ; Plant Proteins/chemistry/genetics/*physiology ; Polymerase Chain Reaction ; Polymorphism, Single Nucleotide ; Protein Structure, Tertiary
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  • 20
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    Genome of the host-cell transforming parasite Theileria annulata compared with T. parva (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-07-05
    Description: Theileria annulata and T. parva are closely related protozoan parasites that cause lymphoproliferative diseases of cattle. We sequenced the genome of T. annulata and compared it with that of T. parva to understand the mechanisms underlying transformation and tropism. Despite high conservation of gene sequences and synteny, the analysis reveals unequally expanded gene families and species-specific genes. We also identify divergent families of putative secreted polypeptides that may reduce immune recognition, candidate regulators of host-cell transformation, and a Theileria-specific protein domain [frequently associated in Theileria (FAINT)] present in a large number of secreted proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pain, Arnab -- Renauld, Hubert -- Berriman, Matthew -- Murphy, Lee -- Yeats, Corin A -- Weir, William -- Kerhornou, Arnaud -- Aslett, Martin -- Bishop, Richard -- Bouchier, Christiane -- Cochet, Madeleine -- Coulson, Richard M R -- Cronin, Ann -- de Villiers, Etienne P -- Fraser, Audrey -- Fosker, Nigel -- Gardner, Malcolm -- Goble, Arlette -- Griffiths-Jones, Sam -- Harris, David E -- Katzer, Frank -- Larke, Natasha -- Lord, Angela -- Maser, Pascal -- McKellar, Sue -- Mooney, Paul -- Morton, Fraser -- Nene, Vishvanath -- O'Neil, Susan -- Price, Claire -- Quail, Michael A -- Rabbinowitsch, Ester -- Rawlings, Neil D -- Rutter, Simon -- Saunders, David -- Seeger, Kathy -- Shah, Trushar -- Squares, Robert -- Squares, Steven -- Tivey, Adrian -- Walker, Alan R -- Woodward, John -- Dobbelaere, Dirk A E -- Langsley, Gordon -- Rajandream, Marie-Adele -- McKeever, Declan -- Shiels, Brian -- Tait, Andrew -- Barrell, Bart -- Hall, Neil -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):131-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA, UK. ap2@sanger.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994557" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Cattle ; Cell Proliferation ; Chromosome Mapping ; Chromosomes/genetics ; Conserved Sequence ; Genes, Protozoan ; *Genome, Protozoan ; Life Cycle Stages ; Lipid Metabolism ; Lymphocytes/cytology/parasitology ; Molecular Sequence Data ; Multigene Family ; Phylogeny ; Protein Sorting Signals/genetics ; Protein Structure, Tertiary ; Proteome ; Protozoan Proteins/chemistry/*genetics/physiology ; Sequence Analysis, DNA ; Species Specificity ; Synteny ; Telomere/genetics ; Theileria annulata/*genetics/growth & development/immunology/pathogenicity ; Theileria parva/*genetics/growth & development/immunology/pathogenicity
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  • 21
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    Structural biology. A dearth of new folds (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1555.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761137" target="_blank"〉PubMed〈/a〉
    Keywords: *Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry/genetics
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  • 22
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    Apolipoprotein L-I promotes trypanosome lysis by forming pores in lysosomal membranes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: Apolipoprotein L-I is the trypanolytic factor of human serum. Here we show that this protein contains a membrane pore-forming domain functionally similar to that of bacterial colicins, flanked by a membrane-addressing domain. In lipid bilayer membranes, apolipoprotein L-I formed anion channels. In Trypanosoma brucei, apolipoprotein L-I was targeted to the lysosomal membrane and triggered depolarization of this membrane, continuous influx of chloride, and subsequent osmotic swelling of the lysosome until the trypanosome lysed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perez-Morga, David -- Vanhollebeke, Benoit -- Paturiaux-Hanocq, Francoise -- Nolan, Derek P -- Lins, Laurence -- Homble, Fabrice -- Vanhamme, Luc -- Tebabi, Patricia -- Pays, Annette -- Poelvoorde, Philippe -- Jacquet, Alain -- Brasseur, Robert -- Pays, Etienne -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):469-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Parasitology, IBMM, Universite Libre de Bruxelles, 12, rue des Profs Jeener et Brachet, B6041 Gosselies, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020735" target="_blank"〉PubMed〈/a〉
    Keywords: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid/pharmacology ; Amino Acid Sequence ; Animals ; Anions/metabolism ; Apolipoproteins/*chemistry/genetics/*metabolism/pharmacology ; Cells, Immobilized ; Chlorides/metabolism ; Colicins/chemistry/pharmacology ; Escherichia coli/drug effects/growth & development ; Humans ; Intracellular Membranes/drug effects/*metabolism/ultrastructure ; Ion Channels/metabolism ; Lipid Bilayers/chemistry ; Lipoproteins, HDL/*chemistry/genetics/*metabolism/pharmacology ; Lysosomes/drug effects/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Permeability ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/metabolism ; Trypanosoma brucei brucei/drug effects/*metabolism/ultrastructure
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  • 23
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    OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-05
    Description: Oxysterol-binding protein (OSBP) is the founding member of a family of sterol-binding proteins implicated in vesicle transport, lipid metabolism, and signal transduction. Here, OSBP was found to function as a cholesterol-binding scaffolding protein coordinating the activity of two phosphatases to control the extracellular signal-regulated kinase (ERK) signaling pathway. Cytosolic OSBP formed a approximately 440-kilodalton oligomer with a member of the PTPPBS family of tyrosine phosphatases, the serine/threonine phosphatase PP2A, and cholesterol. This oligomer had dual specific phosphatase activity for phosphorylated ERK (pERK). When cell cholesterol was lowered, the oligomer disassembled and the level of pERK rose. The oligomer also disassembled when exposed to oxysterols. Increasing the amount of OSBP oligomer rendered cells resistant to the effects of cholesterol depletion and decreased the basal level of pERK. Thus, cholesterol functions through its interaction with OSBP outside of membranes to regulate the assembly of an oligomeric phosphatase that controls a key signaling pathway in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Ping-Yuan -- Weng, Jian -- Anderson, Richard G W -- GM 52016/GM/NIGMS NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1472-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746430" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cholesterol/*metabolism ; Cytosol/metabolism ; Enzyme Activation ; HeLa Cells ; Humans ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase 1/*metabolism ; Mitogen-Activated Protein Kinase 3/*metabolism ; Multiprotein Complexes/metabolism ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Conformation ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/metabolism ; RNA Interference ; Receptors, Steroid/chemistry/genetics/*metabolism ; Transfection ; beta-Cyclodextrins/pharmacology
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    Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: Ubiquitination controls a broad range of cellular functions. The last step of the ubiquitination pathway is regulated by enzyme type 3 (E3) ubiquitin ligases. E3 enzymes are responsible for substrate specificity and catalyze the formation of an isopeptide bond between a lysine residue of the substrate (or the N terminus of the substrate) and ubiquitin. MIR1 and MIR2 are two E3 ubiquitin ligases encoded by Kaposi's sarcoma-associated herpesvirus that mediate the ubiquitination of major histocompatibility complex class I (MHC I) molecules and subsequent internalization. Here, we found that MIR1, but not MIR2, promoted down-regulation of MHC I molecules lacking lysine residues in their intracytoplasmic domain. In the presence of MIR1, these MHC I molecules were ubiquitinated, and their association with ubiquitin was sensitive to beta2-mercaptoethanol, unlike lysine-ubiquitin bonds. This form of ubiquitination required a cysteine residue in the intracytoplasmic tail of MHC I molecules. An MHC I molecule containing a single cysteine residue in an artificial glycine and alanine intracytoplasmic domain was endocytosed and degraded in the presence of MIR1. Thus, ubiquitination can occur on proteins lacking accessible lysines or an accessible N terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cadwell, Ken -- Coscoy, Laurent -- 1R01CA108447-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):127-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, 142 Life Sciences Addition Room 3200, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; CHO Cells ; Cell Line ; Cricetinae ; Cysteine/chemistry/metabolism ; Down-Regulation ; Endocytosis ; HLA-B7 Antigen/chemistry/genetics/*metabolism ; Herpesvirus 8, Human/*enzymology ; Humans ; Lysine/metabolism ; Mutation ; Protein Structure, Tertiary ; Serine/chemistry/metabolism ; Transduction, Genetic ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligases/*metabolism
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    Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-02
    Description: The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murata, Takeshi -- Yamato, Ichiro -- Kakinuma, Yoshimi -- Leslie, Andrew G W -- Walker, John E -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):654-9. Epub 2005 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802565" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Detergents/metabolism ; Enterococcus/*enzymology ; Ion Transport ; Models, Biological ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Molecular Sequence Data ; Phospholipids/chemistry/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Sodium/metabolism ; Static Electricity ; Water
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structure of a synaptic gammadelta resolvase tetramer covalently linked to two cleaved DNAs (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: The structure of a synaptic intermediate of the site-specific recombinase gammadelta resolvase covalently linked through Ser10 to two cleaved duplex DNAs has been determined at 3.4 angstrom resolution. This resolvase, activated for recombination by mutations, forms a tetramer whose structure is substantially changed from that of a presynaptic complex between dimeric resolvase and the cleavage site DNA. Because the two cleaved DNA duplexes that are to be recombined lie on opposite sides of the core tetramer, large movements of both protein and DNA are required to achieve strand exchange. The two dimers linked to the DNAs that are to be recombined are held together by a flat interface. This may allow a 180 degrees rotation of one dimer relative to the other in order to reposition the DNA duplexes for strand exchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Weikai -- Kamtekar, Satwik -- Xiong, Yong -- Sarkis, Gary J -- Grindley, Nigel D F -- Steitz, Thomas A -- GM28470/GM/NIGMS NIH HHS/ -- GM57510/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 19;309(5738):1210-5. Epub 2005 Jun 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994378" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Binding Sites ; Catalytic Domain ; Computer Simulation ; Crystallography, X-Ray ; DNA/*chemistry/*metabolism ; Dimerization ; Models, Molecular ; Mutation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombination, Genetic ; Transposon Resolvases/*chemistry/genetics/metabolism
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    Allosteric mechanisms of signal transduction (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-04
    Description: Forty years ago, a simple model of allosteric mechanisms (indirect interactions between distinct sites), used initially to explain feedback-inhibited enzymes, was presented by Monod, Wyman, and Changeux. We review the MWC theory and its applications for the understanding of signal transduction in biology, and also identify remaining issues that deserve theoretical and experimental substantiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, Jean-Pierre -- Edelstein, Stuart J -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1424-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Receptors and Cognition, Institut Pasteur, 75724 Paris Cedex 15, France. changeux@pasteur.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933191" target="_blank"〉PubMed〈/a〉
    Keywords: *Allosteric Regulation ; Binding Sites ; Enzymes/metabolism ; Ligands ; Models, Biological ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Cell Surface/physiology ; Signal Transduction/*physiology
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    Structure of the ABC transporter MsbA in complex with ADP.vanadate and lipopolysaccharide (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-14
    Description: Select members of the adenosine triphosphate (ATP)-binding cassette (ABC) transporter family couple ATP binding and hydrolysis to substrate efflux and confer multidrug resistance. We have determined the x-ray structure of MsbA in complex with magnesium, adenosine diphosphate, and inorganic vanadate (Mg.ADP.Vi) and the rough-chemotype lipopolysaccharide, Ra LPS. The structure supports a model involving a rigid-body torque of the two transmembrane domains during ATP hydrolysis and suggests a mechanism by which the nucleotide-binding domain communicates with the transmembrane domain. We propose a lipid "flip-flop" mechanism in which the sugar groups are sequestered in the chamber while the hydrophobic tails are dragged through the lipid bilayer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reyes, Christopher L -- Chang, Geoffrey -- GM61905/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 13;308(5724):1028-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road CB105, La Jolla, CA 92137, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890884" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/*metabolism ; Adenosine Diphosphate/*metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Bacterial Proteins/*chemistry/*metabolism ; Binding Sites ; Cell Membrane/*chemistry ; Crystallography, X-Ray ; Cytoplasm/chemistry ; Dimerization ; Fourier Analysis ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers ; Lipopolysaccharides/*metabolism ; Magnesium/metabolism ; Models, Molecular ; Periplasm/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Salmonella typhimurium/*chemistry ; Substrate Specificity ; Vanadates/*metabolism
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    Crystal structure of a mammalian voltage-dependent Shaker family K+ channel (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-09
    Description: Voltage-dependent potassium ion (K+) channels (Kv channels) conduct K+ ions across the cell membrane in response to changes in the membrane voltage, thereby regulating neuronal excitability by modulating the shape and frequency of action potentials. Here we report the crystal structure, at a resolution of 2.9 angstroms, of a mammalian Kv channel, Kv1.2, which is a member of the Shaker K+ channel family. This structure is in complex with an oxido-reductase beta subunit of the kind that can regulate mammalian Kv channels in their native cell environment. The activation gate of the pore is open. Large side portals communicate between the pore and the cytoplasm. Electrostatic properties of the side portals and positions of the T1 domain and beta subunit are consistent with electrophysiological studies of inactivation gating and with the possibility of K+ channel regulation by the beta subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Long, Stephen B -- Campbell, Ernest B -- Mackinnon, Roderick -- GM43949/GM/NIGMS NIH HHS/ -- RR00862/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):897-903. Epub 2005 Jul 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16002581" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalytic Domain ; Cloning, Molecular ; Crystallography, X-Ray ; Electrochemistry ; Kv1.2 Potassium Channel ; Models, Molecular ; Pichia ; Potassium/chemistry ; Potassium Channels, Voltage-Gated/*chemistry ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Rats ; Recombinant Proteins/chemistry
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    An acylation cycle regulates localization and activity of palmitoylated Ras isoforms (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-12
    Description: We show that the specific subcellular distribution of H- and Nras guanosine triphosphate-binding proteins is generated by a constitutive de/reacylation cycle that operates on palmitoylated proteins, driving their rapid exchange between the plasma membrane (PM) and the Golgi apparatus. Depalmitoylation redistributes farnesylated Ras in all membranes, followed by repalmitoylation and trapping of Ras at the Golgi, from where it is redirected to the PM via the secretory pathway. This continuous cycle prevents Ras from nonspecific residence on endomembranes, thereby maintaining the specific intracellular compartmentalization. The de/reacylation cycle also initiates Ras activation at the Golgi by transport of PM-localized Ras guanosine triphosphate. Different de/repalmitoylation kinetics account for isoform-specific activation responses to growth factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rocks, Oliver -- Peyker, Anna -- Kahms, Martin -- Verveer, Peter J -- Koerner, Carolin -- Lumbierres, Maria -- Kuhlmann, Jurgen -- Waldmann, Herbert -- Wittinghofer, Alfred -- Bastiaens, Philippe I H -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1746-52. Epub 2005 Feb 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Max Planck Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15705808" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Animals ; COS Cells ; Cell Line ; Cell Membrane/*metabolism ; Cercopithecus aethiops ; Dogs ; Golgi Apparatus/*metabolism ; Guanosine Triphosphate/metabolism ; Kinetics ; Models, Biological ; Molecular Sequence Data ; Palmitic Acid/*metabolism ; Protein Isoforms/chemistry/metabolism ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Protein Transport ; Proto-Oncogene Proteins p21(ras)/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    Structural biology. Adaptation of SARS coronavirus to humans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, Kathryn V -- AI59578/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1822-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Colorado Health Sciences Center, Mail Stop 8333, Post Office Box 6211, Aurora, CO 80045, USA. kathryn.holmes@uchsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166506" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Substitution ; Animals ; Binding Sites ; Carboxypeptidases/*chemistry/metabolism ; Disease Outbreaks ; Genes, Viral ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/*chemistry/genetics/metabolism ; Mutation ; Peptidyl-Dipeptidase A ; Protein Structure, Tertiary ; RNA, Viral/genetics ; Receptors, Virus/*chemistry/metabolism ; Recombination, Genetic ; SARS Virus/*chemistry/*genetics/physiology ; Severe Acute Respiratory Syndrome/epidemiology/prevention & control/*virology ; Species Specificity ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/*chemistry/genetics/metabolism ; Viral Vaccines ; Virus Replication ; Viverridae/virology
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    Structure of a V3-containing HIV-1 gp120 core (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-15
    Description: The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is immunodominant and contains features essential for coreceptor binding. We determined the structure of V3 in the context of an HIV-1 gp120 core complexed to the CD4 receptor and to the X5 antibody at 3.5 angstrom resolution. Binding of gp120 to cell-surface CD4 would position V3 so that its coreceptor-binding tip protrudes 30 angstroms from the core toward the target cell membrane. The extended nature and antibody accessibility of V3 explain its immunodominance. Together, the results provide a structural rationale for the role of V3 in HIV entry and neutralization.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2408531/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2408531/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Chih-chin -- Tang, Min -- Zhang, Mei-Yun -- Majeed, Shahzad -- Montabana, Elizabeth -- Stanfield, Robyn L -- Dimitrov, Dimiter S -- Korber, Bette -- Sodroski, Joseph -- Wilson, Ian A -- Wyatt, Richard -- Kwong, Peter D -- AI24755/AI/NIAID NIH HHS/ -- AI31783/AI/NIAID NIH HHS/ -- AI39429/AI/NIAID NIH HHS/ -- AI40895/AI/NIAID NIH HHS/ -- GM46192/GM/NIGMS NIH HHS/ -- Z99 AI999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):1025-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD4/chemistry/*metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; HIV Antibodies/immunology ; HIV Envelope Protein gp120/*chemistry/immunology/metabolism ; HIV-1/*chemistry/immunology/metabolism ; Humans ; Hydrogen Bonding ; Immunodominant Epitopes ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments/*chemistry/immunology/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, CCR5/chemistry/metabolism ; Receptors, CXCR4/chemistry/metabolism
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    Genome sequence of Theileria parva, a bovine pathogen that transforms lymphocytes (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: We report the genome sequence of Theileria parva, an apicomplexan pathogen causing economic losses to smallholder farmers in Africa. The parasite chromosomes exhibit limited conservation of gene synteny with Plasmodium falciparum, and its plastid-like genome represents the first example where all apicoplast genes are encoded on one DNA strand. We tentatively identify proteins that facilitate parasite segregation during host cell cytokinesis and contribute to persistent infection of transformed host cells. Several biosynthetic pathways are incomplete or absent, suggesting substantial metabolic dependence on the host cell. One protein family that may generate parasite antigenic diversity is not telomere-associated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardner, Malcolm J -- Bishop, Richard -- Shah, Trushar -- de Villiers, Etienne P -- Carlton, Jane M -- Hall, Neil -- Ren, Qinghu -- Paulsen, Ian T -- Pain, Arnab -- Berriman, Matthew -- Wilson, Robert J M -- Sato, Shigeharu -- Ralph, Stuart A -- Mann, David J -- Xiong, Zikai -- Shallom, Shamira J -- Weidman, Janice -- Jiang, Lingxia -- Lynn, Jeffery -- Weaver, Bruce -- Shoaibi, Azadeh -- Domingo, Alexander R -- Wasawo, Delia -- Crabtree, Jonathan -- Wortman, Jennifer R -- Haas, Brian -- Angiuoli, Samuel V -- Creasy, Todd H -- Lu, Charles -- Suh, Bernard -- Silva, Joana C -- Utterback, Teresa R -- Feldblyum, Tamara V -- Pertea, Mihaela -- Allen, Jonathan -- Nierman, William C -- Taracha, Evans L N -- Salzberg, Steven L -- White, Owen R -- Fitzhugh, Henry A -- Morzaria, Subhash -- Venter, J Craig -- Fraser, Claire M -- Nene, Vishvanath -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research (TIGR), 9712 Medical Center Drive, Rockville, MD 20850, USA. gardner@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994558" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Antigens, Protozoan/genetics ; Cattle ; Cell Proliferation ; Chromosomes/genetics ; Conserved Sequence ; Enzymes/genetics/metabolism ; Genes, Protozoan ; *Genome, Protozoan ; Lymphocytes/cytology/*parasitology ; Mitochondria/metabolism ; Molecular Sequence Data ; Organelles/genetics/physiology ; Plasmodium falciparum/genetics ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry/*genetics/metabolism ; Sequence Analysis, DNA ; Synteny ; Telomere/genetics ; Theileria parva/*genetics/growth & development/pathogenicity/physiology
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    Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-30
    Description: In the crystal structure of the membrane-embedded rotor ring of the sodium ion-translocating adenosine 5'-triphosphate (ATP) synthase of Ilyobacter tartaricus at 2.4 angstrom resolution, 11 c subunits are assembled into an hourglass-shaped cylinder with 11-fold symmetry. Sodium ions are bound in a locked conformation close to the outer surface of the cylinder near the middle of the membrane. The structure supports an ion-translocation mechanism in the intact ATP synthase in which the binding site converts from the locked conformation into one that opens toward subunit a as the rotor ring moves through the subunit a/c interface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meier, Thomas -- Polzer, Patrick -- Diederichs, Kay -- Welte, Wolfram -- Dimroth, Peter -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):659-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Mikrobiologie, Eidgenossische Technische Hochschule (ETH), Zurich Honggerberg, Wolfgang-Pauli-Str. 10, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860619" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Cytoplasm/metabolism ; Fusobacteria/*enzymology ; Glutamic Acid/chemistry/metabolism ; Hydrophobic and Hydrophilic Interactions ; Ion Transport ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Sodium/metabolism
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    Structural biology. Nature's rotary electromotors (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Junge, Wolfgang -- Nelson, Nathan -- New York, N.Y. -- Science. 2005 Apr 29;308(5722):642-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biophysics, University of Osnabruck, 49069 Osnabruck, Germany. junge@uos.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860615" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Electrochemistry ; Enterococcus/*enzymology ; Fusobacteria/*enzymology ; Glutamic Acid/chemistry/metabolism ; Hydrogen-Ion Concentration ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Sodium/metabolism ; Static Electricity
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    Extensive diversity of Ig-superfamily proteins in the immune system of insects (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-08-20
    Description: The extensive somatic diversification of immune receptors is a hallmark of higher vertebrates. However, whether molecular diversity contributes to immune protection in invertebrates is unknown. We present evidence that Drosophila immune-competent cells have the potential to express more than 18,000 isoforms of the immunoglobulin (Ig)-superfamily receptor Down syndrome cell adhesion molecule (Dscam). Secreted protein isoforms of Dscam were detected in the hemolymph, and hemocyte-specific loss of Dscam impaired the efficiency of phagocytic uptake of bacteria, possibly due to reduced bacterial binding. Importantly, the molecular diversity of Dscam transcripts generated through a mechanism of alternative splicing is highly conserved across major insect orders, suggesting an unsuspected molecular complexity of the innate immune system of insects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watson, Fiona L -- Puttmann-Holgado, Roland -- Thomas, Franziska -- Lamar, David L -- Hughes, Michael -- Kondo, Masahiro -- Rebel, Vivienne I -- Schmucker, Dietmar -- 1RO1-NS46747-01/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1874-8. Epub 2005 Aug 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Dana Farber Cancer Institute, Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16109846" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Brain/metabolism ; Cell Adhesion Molecules ; Cell Line ; Drosophila Proteins/chemistry/*genetics/*immunology/metabolism ; Drosophila melanogaster/*genetics/*immunology/metabolism ; Escherichia coli/immunology/metabolism ; Fat Body/metabolism ; Hemocytes/immunology/*metabolism ; Hemolymph/chemistry ; Immunity, Innate ; Immunoglobulins/chemistry ; Insects/chemistry/genetics ; Molecular Sequence Data ; Neurons/metabolism ; Oligonucleotide Array Sequence Analysis ; Phagocytosis ; Protein Isoforms/chemistry/genetics/metabolism ; Protein Structure, Tertiary ; RNA Interference ; Receptors, Immunologic/immunology/metabolism
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    Structural basis of energy transduction in the transport cycle of MsbA (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-14
    Description: We used site-directed spin-labeling and electron paramagnetic resonance spectroscopy to characterize the conformational motion that couples energy expenditure to substrate translocation in the multidrug transporter MsbA. In liposomes, ligand-free MsbA samples conformations that depart from the crystal structures, including looser packing and water penetration along the periplasmic side. Adenosine triphosphate (ATP) binding closes the substrate chamber to the cytoplasm while increasing hydration at the periplasmic side, consistent with an alternating access model. Accentuated by ATP hydrolysis, the changes in the chamber dielectric environment and its geometry provide the likely driving force for flipping amphipathic substrates and a potential exit pathway. These results establish the structural dynamic basis of the power stroke in multidrug-resistant ATP-binding cassette (MDR ABC) transporters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, Jinhui -- Yang, Guangyong -- McHaourab, Hassane S -- New York, N.Y. -- Science. 2005 May 13;308(5724):1023-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890883" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/*metabolism ; Adenosine Triphosphate/*metabolism ; Apoproteins/chemistry/metabolism ; Bacterial Proteins/*chemistry/*metabolism ; Biological Transport ; Cell Membrane/chemistry/metabolism ; Cytoplasm/chemistry ; Dimerization ; Edetic Acid/*analogs & derivatives ; Electron Spin Resonance Spectroscopy ; *Energy Metabolism ; Escherichia coli Proteins/chemistry/metabolism ; Hydrolysis ; Ligands ; Lipid A/metabolism ; Lipid Bilayers ; Liposomes/*chemistry ; Models, Molecular ; Oxygen/metabolism ; Periplasm/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Spin Labels ; Thermodynamics ; Vanadates/metabolism
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    Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pufall, Miles A -- Lee, Gregory M -- Nelson, Mary L -- Kang, Hyun-Seo -- Velyvis, Algirdas -- Kay, Lewis E -- McIntosh, Lawrence P -- Graves, Barbara J -- GM08537/GM/NIGMS NIH HHS/ -- P01-CA24014/CA/NCI NIH HHS/ -- R01 GM38663/GM/NIGMS NIH HHS/ -- T32-CA93247/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):142-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Huntsman Cancer Institute, Department of Oncological Sciences, University of Utah, Salt Lake City, UT 84112-5550, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994560" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; DNA/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/*chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-ets ; Signal Transduction ; Transcription Factors/*chemistry/genetics/*metabolism
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    Supramolecular assembly of amelogenin nanospheres into birefringent microribbons (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-05
    Description: Although both tooth enamel and bone are composed of organized assemblies of carbonated apatite crystals, enamel is unusual in that it does not contain collagen nor does it remodel. Self-assembly of amelogenin protein into nanospheres has been recognized as a key factor in controlling the oriented and elongated growth of carbonated apatite crystals during dental enamel biomineralization. We report the in vitro formation of birefringent microribbon structures that were generated through the supramolecular assembly of amelogenin nanospheres. These microribbons have diffraction patterns that indicate a periodic structure of crystalline units along the long axis. The growth of apatite crystals orientated along the c axis and parallel to the long axes of the microribbons was observed in vitro. The linear arrays (chains) of nanospheres observed as intermediate states before the microribbon formation give an important indication as to the function of amelogenin in controlling the oriented growth of apatite crystals during enamel mineralization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Du, Chang -- Falini, Giuseppe -- Fermani, Simona -- Abbott, Christopher -- Moradian-Oldak, Janet -- R01 DE013414/DE/NIDCR NIH HHS/ -- R01-DE-13414/DE/NIDCR NIH HHS/ -- R21-DE-15332/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1450-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, 2250 Alcazar Street, CSA 103, Los Angeles, CA 90033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746422" target="_blank"〉PubMed〈/a〉
    Keywords: *Amelogenesis ; Amelogenin ; Animals ; Birefringence ; Crystallization ; Dental Enamel Proteins/*chemistry/metabolism ; Durapatite/chemistry ; Hydrophobic and Hydrophilic Interactions ; Microscopy, Atomic Force ; Microscopy, Electron ; *Nanotubes ; Phosvitin ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Swine ; X-Ray Diffraction
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    Immunology. Close to the edge: neutralizing the HIV-1 envelope (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nabel, Gary J -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1878-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center (VRC), National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. gnabel@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976295" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/therapeutic use ; Animals ; Antibodies, Monoclonal/immunology/therapeutic use ; Antibody Specificity ; Autoantigens/immunology ; Autoimmune Diseases/immunology ; Cardiolipins/*immunology ; Complementarity Determining Regions ; Epitopes ; Gene Products, env/chemistry/*immunology ; HIV Antibodies/chemistry/genetics/*immunology/therapeutic use ; HIV Envelope Protein gp41/chemistry/*immunology ; HIV Infections/*immunology/prevention & control/therapy ; HIV-1/*immunology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Immunization, Passive ; Models, Molecular ; Mutation ; Neutralization Tests ; Protein Structure, Tertiary
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    Protein structures forming the shell of primitive bacterial organelles (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-08-06
    Description: Bacterial microcompartments are primitive organelles composed entirely of protein subunits. Genomic sequence databases reveal the widespread occurrence of microcompartments across diverse microbes. The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. We report three-dimensional crystal structures of multiple carboxysome shell proteins, revealing a hexameric unit as the basic microcompartment building block and showing how these hexamers assemble to form flat facets of the polyhedral shell. The structures suggest how molecular transport across the shell may be controlled and how structural variations might govern the assembly and architecture of these subcellular compartments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerfeld, Cheryl A -- Sawaya, Michael R -- Tanaka, Shiho -- Nguyen, Chau V -- Phillips, Martin -- Beeby, Morgan -- Yeates, Todd O -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):936-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles (UCLA), Box 951570, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16081736" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Organelles/*chemistry ; Protein Conformation ; Protein Structure, Tertiary ; Sequence Alignment ; Synechocystis/*chemistry/ultrastructure
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    Rev1 employs a novel mechanism of DNA synthesis using a protein template (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-01
    Description: The Rev1 DNA polymerase is highly specialized for the incorporation of C opposite template G. We present here the crystal structure of yeast Rev1 bound to template G and incoming 2'-deoxycytidine 5'-triphosphate (dCTP), which reveals that the polymerase itself dictates the identity of the incoming nucleotide, as well as the identity of the templating base. Template G and incoming dCTP do not pair with each other. Instead, the template G is evicted from the DNA helix, and it makes optimal hydrogen bonds with a segment of Rev1. Also, unlike other DNA polymerases, incoming dCTP pairs with an arginine rather than the templating base, which ensures the incorporation of dCTP over other incoming nucleotides. This mechanism provides an elegant means for promoting proficient and error-free synthesis through N2-adducted guanines that obstruct replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nair, Deepak T -- Johnson, Robert E -- Prakash, Louise -- Prakash, Satya -- Aggarwal, Aneel K -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine, Box 1677, 1425 Madison Avenue, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195463" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/metabolism ; Base Pairing ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; *DNA Replication ; DNA, Fungal/*biosynthesis ; Deoxycytosine Nucleotides/chemistry/*metabolism ; Guanine/chemistry/*metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Nucleotidyltransferases/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/enzymology/metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism ; Templates, Genetic
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    Voltage sensor of Kv1.2: structural basis of electromechanical coupling (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-07-09
    Description: Voltage-dependent ion channels contain voltage sensors that allow them to switch between nonconductive and conductive states over the narrow range of a few hundredths of a volt. We investigated the mechanism by which these channels sense cell membrane voltage by determining the x-ray crystal structure of a mammalian Shaker family potassium ion (K+) channel. The voltage-dependent K+ channel Kv1.2 grew three-dimensional crystals, with an internal arrangement that left the voltage sensors in an apparently native conformation, allowing us to reach three important conclusions. First, the voltage sensors are essentially independent domains inside the membrane. Second, they perform mechanical work on the pore through the S4-S5 linker helices, which are positioned to constrict or dilate the S6 inner helices of the pore. Third, in the open conformation, two of the four conserved Arg residues on S4 are on a lipid-facing surface and two are buried in the voltage sensor. The structure offers a simple picture of how membrane voltage influences the open probability of the channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Long, Stephen B -- Campbell, Ernest B -- Mackinnon, Roderick -- GM43949/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):903-8. Epub 2005 Jul 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16002579" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry ; Crystallography, X-Ray ; Electrochemistry ; Ion Channel Gating/physiology ; Membrane Potentials ; Models, Biological ; Models, Molecular ; Potassium Channels/*chemistry/*physiology ; Protein Conformation ; Protein Structure, Tertiary ; Structure-Activity Relationship
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  • 44
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    Organization of iron-sulfur clusters in respiratory complex I (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-30
    Description: Complex I of respiratory chains plays a central role in bioenergetics and is implicated in many human neurodegenerative diseases. An understanding of its mechanism requires a knowledge of the organization of redox centers. The arrangement of iron-sulfur clusters in the hydrophilic domain of complex I from Thermus thermophilus has been determined with the use of x-ray crystallography. One binuclear and six tetranuclear clusters are arranged, maximally 14 angstroms apart, in an 84-angstrom-long electron transfer chain. The binuclear cluster N1a and the tetranuclear cluster N7 are not in this pathway. Cluster N1a may play a role in the prevention of oxidative damage. The structure provides a framework for the interpretation of the large amounts of data accumulated on complex I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinchliffe, Philip -- Sazanov, Leonid A -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):771-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051796" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Electron Transport ; Electron Transport Complex I/*chemistry/isolation & purification/metabolism ; Flavin Mononucleotide/metabolism ; Iron/*chemistry ; Models, Molecular ; NAD/metabolism ; Oxidation-Reduction ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/isolation & purification/metabolism ; Sulfur/*chemistry ; Thermus thermophilus/*enzymology
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    PUMA couples the nuclear and cytoplasmic proapoptotic function of p53 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-10
    Description: The Trp53 tumor suppressor gene product (p53) functions in the nucleus to regulate proapoptotic genes, whereas cytoplasmic p53 directly activates proapoptotic Bcl-2 proteins to permeabilize mitochondria and initiate apoptosis. Here, we demonstrate that a tripartite nexus between Bcl-xL, cytoplasmic p53, and PUMA coordinates these distinct p53 functions. After genotoxic stress, Bcl-xL sequestered cytoplasmic p53. Nuclear p53 caused expression of PUMA, which then displaced p53 from Bcl-xL, allowing p53 to induce mitochondrial permeabilization. Mutant Bcl-xL that bound p53, but not PUMA, rendered cells resistant to p53-induced apoptosis irrespective of PUMA expression. Thus, PUMA couples the nuclear and cytoplasmic proapoptotic functions of p53.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chipuk, Jerry E -- Bouchier-Hayes, Lisa -- Kuwana, Tomomi -- Newmeyer, Donald D -- Green, Douglas R -- New York, N.Y. -- Science. 2005 Sep 9;309(5741):1732-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular Immunology, La Jolla Institute for Allergy and Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16151013" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptosis Regulatory Proteins ; Cell Line, Tumor ; Cell Nucleus/*metabolism ; Cells, Cultured ; Cytoplasm/*metabolism ; DNA Damage ; Gene Expression Regulation ; Humans ; Immunoprecipitation ; Mice ; Mice, Inbred C57BL ; Mitochondria/metabolism ; Models, Biological ; Permeability ; Protein Binding ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Recombinant Proteins/metabolism ; Tumor Suppressor Protein p53/*metabolism ; Tumor Suppressor Proteins/chemistry/*metabolism ; Ultraviolet Rays ; bcl-2-Associated X Protein ; bcl-X Protein
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    Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-05
    Description: The 2.0-angstrom structure of the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) catalytic subunit bound to a deletion mutant of a regulatory subunit (RIalpha) defines a previously unidentified extended interface. The complex provides a molecular mechanism for inhibition of PKA and suggests how cAMP binding leads to activation. The interface defines the large lobe of the catalytic subunit as a stable scaffold where Tyr247 in the G helix and Trp196 in the phosphorylated activation loop serve as anchor points for binding RIalpha. These residues compete with cAMP for the phosphate binding cassette in RIalpha. In contrast to the catalytic subunit, RIalpha undergoes major conformational changes when the complex is compared with cAMP-bound RIalpha. The inhibitor sequence docks to the active site, whereas the linker, also disordered in free RIalpha, folds across the extended interface. The beta barrel of cAMP binding domain A, which is the docking site for cAMP, remains largely intact in the complex, whereas the helical subdomain undergoes major reorganization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Choel -- Xuong, Nguyen-Huu -- Taylor, Susan S -- DK07233/DK/NIDDK NIH HHS/ -- GM19301/GM/NIGMS NIH HHS/ -- GM34921/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):690-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692043" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinase RIalpha Subunit ; Cyclic AMP-Dependent Protein Kinases/antagonists & ; inhibitors/*chemistry/*metabolism ; Enzyme Activation ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Tryptophan/chemistry ; Tyrosine/chemistry
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-13
    Description: G protein-coupled receptor kinase 2 (GRK2) plays a key role in the desensitization of G protein-coupled receptor signaling by phosphorylating activated heptahelical receptors and by sequestering heterotrimeric G proteins. We report the atomic structure of GRK2 in complex with Galphaq and Gbetagamma, in which the activated Galpha subunit of Gq is fully dissociated from Gbetagamma and dramatically reoriented from its position in the inactive Galphabetagamma heterotrimer. Galphaq forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tesmer, Valerie M -- Kawano, Takeharu -- Shankaranarayanan, Aruna -- Kozasa, Tohru -- Tesmer, John J G -- AG006093/AG/NIA NIH HHS/ -- GM61454/GM/NIGMS NIH HHS/ -- HL071818/HL/NHLBI NIH HHS/ -- NS41441/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1686-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339447" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cattle ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits, Gq-G11/*chemistry/metabolism ; GTP-Binding Protein beta Subunits/*chemistry/metabolism ; GTP-Binding Protein gamma Subunits/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; RGS Proteins/metabolism ; Signal Transduction ; beta-Adrenergic Receptor Kinases/*chemistry/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-14
    Description: Class III adenylyl cyclases contain catalytic and regulatory domains, yet structural insight into their interactions is missing. We show that the mycobacterial adenylyl cyclase Rv1264 is rendered a pH sensor by its N-terminal domain. In the structure of the inhibited state, catalytic and regulatory domains share a large interface involving catalytic residues. In the structure of the active state, the two catalytic domains rotate by 55 degrees to form two catalytic sites at their interface. Two alpha helices serve as molecular switches. Mutagenesis is consistent with a regulatory role of the structural transition, and we suggest that the transition is regulated by pH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tews, Ivo -- Findeisen, Felix -- Sinning, Irmgard -- Schultz, Anita -- Schultz, Joachim E -- Linder, Jurgen U -- New York, N.Y. -- Science. 2005 May 13;308(5724):1020-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemiezentrum der Universitat Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. ivo.tews@bzh.uni-heidelberg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15890882" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases/*chemistry/genetics/*metabolism ; Amino Acid Sequence ; Bacterial Proteins/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Catalytic Domain ; Chemistry, Physical ; Crystallography, X-Ray ; Dimerization ; Holoenzymes/chemistry/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Mycobacterium tuberculosis/*enzymology ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Structure of PTB bound to RNA: specific binding and implications for splicing regulation (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-09-24
    Description: The polypyrimidine tract binding protein (PTB) is a 58-kilodalton RNA binding protein involved in multiple aspects of messenger RNA metabolism, including the repression of alternative exons. We have determined the solution structures of the four RNA binding domains (RBDs) of PTB, each bound to a CUCUCU oligonucleotide. Each RBD binds RNA with a different binding specificity. RBD3 and RBD4 interact, resulting in an antiparallel orientation of their bound RNAs. Thus, PTB will induce RNA looping when bound to two separated pyrimidine tracts within the same RNA. This leads to structural models for how PTB functions as an alternative-splicing repressor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oberstrass, Florian C -- Auweter, Sigrid D -- Erat, Michele -- Hargous, Yann -- Henning, Anke -- Wenter, Philipp -- Reymond, Luc -- Amir-Ahmady, Batoul -- Pitsch, Stefan -- Black, Douglas L -- Allain, Frederic H-T -- New York, N.Y. -- Science. 2005 Sep 23;309(5743):2054-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology, Zurich, ETH-Honggerberg, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16179478" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Exons ; Heterogeneous-Nuclear Ribonucleoproteins/*chemistry/genetics/*metabolism ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Nuclear Proteins/metabolism ; Oligoribonucleotides ; Polypyrimidine Tract-Binding Protein/*chemistry/genetics/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; RNA/*chemistry/*metabolism ; Ribonucleoproteins/metabolism
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    Structural bioinformatics-based design of selective, irreversible kinase inhibitors (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-28
    Description: The active sites of 491 human protein kinase domains are highly conserved, which makes the design of selective inhibitors a formidable challenge. We used a structural bioinformatics approach to identify two selectivity filters, a threonine and a cysteine, at defined positions in the active site of p90 ribosomal protein S6 kinase (RSK). A fluoromethylketone inhibitor, designed to exploit both selectivity filters, potently and selectively inactivated RSK1 and RSK2 in mammalian cells. Kinases with only one selectivity filter were resistant to the inhibitor, yet they became sensitized after genetic introduction of the second selectivity filter. Thus, two amino acids that distinguish RSK from other protein kinases are sufficient to confer inhibitor sensitivity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3641834/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3641834/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Michael S -- Zhang, Chao -- Shokat, Kevan M -- Taunton, Jack -- R01 GM071434-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 27;308(5726):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Chemistry and Chemical Biology, and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143-2280, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15919995" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; COS Cells ; *Computational Biology ; Cysteine/chemistry/metabolism ; Cytidine Deaminase/antagonists & inhibitors/chemistry/metabolism ; Enzyme Inhibitors/*chemistry/metabolism/*pharmacology ; Epidermal Growth Factor/pharmacology ; Heterocyclic Compounds, 2-Ring/chemistry/metabolism/*pharmacology ; Histones/metabolism ; Hydrophobic and Hydrophilic Interactions ; Molecular Structure ; Mutation ; Phosphorylation ; Protein Structure, Tertiary ; Ribosomal Protein S6 Kinases, 90-kDa/*antagonists & ; inhibitors/*chemistry/metabolism ; Sequence Alignment ; Serine/metabolism ; Structure-Activity Relationship ; Threonine/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Mutations in Col4a1 cause perinatal cerebral hemorrhage and porencephaly (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-21
    Description: Porencephaly is a rare neurological disease, typically manifest in infants, which is characterized by the existence of degenerative cavities in the brain. To investigate the molecular pathogenesis of porencephaly, we studied a mouse mutant that develops porencephaly secondary to focal disruptions of vascular basement membranes. Half of the mutant mice died with cerebral hemorrhage within a day of birth, and approximately 18% of survivors had porencephaly. We show that vascular defects are caused by a semidominant mutation in the procollagen type IV alpha 1 gene (Col4a1) in mice, which inhibits the secretion of mutant and normal type IV collagen. We also show that COL4A1 mutations segregate with porencephaly in human families. Because not all mutant mice develop porencephaly, we propose that Col4a1 mutations conspire with environmental trauma in causing the disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gould, Douglas B -- Phalan, F Campbell -- Breedveld, Guido J -- van Mil, Saskia E -- Smith, Richard S -- Schimenti, John C -- Aguglia, Umberto -- van der Knaap, Marjo S -- Heutink, Peter -- John, Simon W M -- CA34196/CA/NCI NIH HHS/ -- EY11721/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2005 May 20;308(5725):1167-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Bar Harbor, ME 04609, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905400" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Animals, Newborn ; Basement Membrane/embryology/metabolism/pathology ; Brain/blood supply/embryology/*pathology ; Brain Diseases/etiology/*genetics/pathology ; Cerebral Hemorrhage/etiology/*genetics/pathology ; Chromosome Mapping ; Collagen Type IV/chemistry/*genetics/metabolism ; Endoderm/metabolism ; Heterozygote ; Humans ; Mice ; *Mutation ; Protein Structure, Tertiary
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    The kinase domain of titin controls muscle gene expression and protein turnover (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-04-02
    Description: The giant sarcomeric protein titin contains a protein kinase domain (TK) ideally positioned to sense mechanical load. We identified a signaling complex where TK interacts with the zinc-finger protein nbr1 through a mechanically inducible conformation. Nbr1 targets the ubiquitin-associated p62/SQSTM1 to sarcomeres, and p62 in turn interacts with MuRF2, a muscle-specific RING-B-box E3 ligase and ligand of the transactivation domain of the serum response transcription factor (SRF). Nuclear translocation of MuRF2 was induced by mechanical inactivity and caused reduction of nuclear SRF and repression of transcription. A human mutation in the titin protein kinase domain causes hereditary muscle disease by disrupting this pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lange, Stephan -- Xiang, Fengqing -- Yakovenko, Andrey -- Vihola, Anna -- Hackman, Peter -- Rostkova, Elena -- Kristensen, Jakob -- Brandmeier, Birgit -- Franzen, Gereon -- Hedberg, Birgitta -- Gunnarsson, Lars Gunnar -- Hughes, Simon M -- Marchand, Sylvie -- Sejersen, Thomas -- Richard, Isabelle -- Edstrom, Lars -- Ehler, Elisabeth -- Udd, Bjarne -- Gautel, Mathias -- G0200496(63216)/Medical Research Council/United Kingdom -- G0300213/Medical Research Council/United Kingdom -- PG/03/049/15364/British Heart Foundation/United Kingdom -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1599-603. Epub 2005 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Muscle Signalling and Development, Randall Division, King's College London, London SE1 1UL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802564" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Catalytic Domain ; Cell Line ; Cell Nucleus/metabolism ; Connectin ; *Gene Expression Regulation ; Heat-Shock Proteins/metabolism ; Humans ; Ligands ; Mice ; Mice, Inbred C3H ; Molecular Sequence Data ; Muscle Proteins/*chemistry/genetics/*metabolism ; Muscle, Skeletal/*metabolism ; Muscular Diseases/genetics ; Mutation ; Myocytes, Cardiac/*metabolism ; Protein Binding ; Protein Conformation ; Protein Kinases/*chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Proteins/metabolism ; Rats ; Respiratory Insufficiency/genetics/metabolism ; Sarcomeres/metabolism ; Serum Response Factor/metabolism ; Signal Transduction ; Two-Hybrid System Techniques ; Ubiquitin-Protein Ligases/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Apoptosis. p53 and PUMA: a deadly duo (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vousden, Karen H -- New York, N.Y. -- Science. 2005 Sep 9;309(5741):1685-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beatson Institute for Cancer Research, Garscube Estate, Switchback Road, Bearsden, Glagsow G61 1BD, UK. k.vousden@beatson.gla.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16151000" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptosis Regulatory Proteins ; Cell Nucleus/*metabolism ; Cytoplasm/*metabolism ; Gene Expression Regulation ; Humans ; Mice ; Mitochondria/metabolism ; Models, Biological ; Mutation ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-bcl-2/genetics/metabolism ; Transcriptional Activation ; Tumor Suppressor Protein p53/*metabolism ; Tumor Suppressor Proteins/chemistry/genetics/*metabolism ; bcl-2-Associated X Protein ; bcl-X Protein
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    A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-24
    Description: The Pseudomonas syringae protein AvrPtoB is translocated into plant cells, where it inhibits immunity-associated programmed cell death (PCD). The structure of a C-terminal domain of AvrPtoB that is essential for anti-PCD activity reveals an unexpected homology to the U-box and RING-finger components of eukaryotic E3 ubiquitin ligases, and we show that AvrPtoB has ubiquitin ligase activity. Mutation of conserved residues involved in the binding of E2 ubiquitin-conjugating enzymes abolishes this activity in vitro, as well as anti-PCD activity in tomato leaves, which dramatically decreases virulence. These results show that Pseudomonas syringae uses a mimic of host E3 ubiquitin ligases to inactivate plant defenses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janjusevic, Radmila -- Abramovitch, Robert B -- Martin, Gregory B -- Stebbins, C Erec -- New York, N.Y. -- Science. 2006 Jan 13;311(5758):222-6. Epub 2005 Dec 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Microbiology, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16373536" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Bacterial Proteins/chemistry/genetics/*metabolism ; Humans ; Lycopersicon esculentum/immunology/*microbiology ; Molecular Mimicry ; Mutagenesis ; Plant Diseases/microbiology ; Plant Leaves/metabolism/microbiology ; Plant Proteins ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases ; Pseudomonas syringae/*enzymology/pathogenicity ; Recombinant Fusion Proteins/genetics/metabolism ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/genetics/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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