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  • Binding Sites  (51)
  • American Association for the Advancement of Science (AAAS)  (51)
  • American Meteorological Society
  • 1995-1999  (51)
  • 1996  (51)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (51)
  • American Meteorological Society
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  • 1995-1999  (51)
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  • 1
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    Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-26
    Description: The SWI/SNF complex participates in the restructuring of chromatin for transcription. The function of the yeast SWI/SNF complex in the remodeling of a nucleosome array has now been analyzed in vitro. Binding of the purified SWI/SNF complex to a nucleosome array disrupted multiple nucleosomes in an adenosine triphosphate-dependent reaction. However, removal of SWI/SNF left a deoxyribonuclease I-hypersensitive site specifically at a nucleosome that was bound by derivatives of the transcription factor Gal4p. Analysis of individual nucleosomes revealed that the SWI/SNF complex catalyzed eviction of histones from the Gal4-bound nucleosomes. Thus, the transient action of the SWI/SNF complex facilitated irreversible disruption of transcription factor-bound nucleosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owen-Hughes, T -- Utley, R T -- Cote, J -- Peterson, C L -- Workman, J L -- GM47867/GM/NIGMS NIH HHS/ -- R01 GM049650/GM/NIGMS NIH HHS/ -- R37 GM049650/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):513-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology and Center for Gene Regulation, Pennsylvania State University, University Park, PA 16802-4500, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662543" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases ; Adenosine Triphosphate/metabolism ; Base Sequence ; Binding Sites ; DNA, Fungal/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Fungal Proteins/*metabolism ; Histones/metabolism ; Molecular Sequence Data ; *Nuclear Proteins ; Nucleosomes/*metabolism/ultrastructure ; Saccharomyces cerevisiae ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*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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  • 2
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    Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: STAT proteins (signal transducers and activators of transcription) activate distinct target genes despite having similar DNA binding preferences. The transcriptional specificity of STAT proteins was investigated on natural STAT binding sites near the interferon-gamma gene. These sites are arranged in multiple copies and required cooperative interactions for STAT binding. The conserved amino-terminal domain of STAT proteins was required for cooperative DNA binding, although this domain was not essential for dimerization or binding to a single site. Cooperative binding interactions enabled the STAT proteins to recognize variations of the consensus site. These sites can be specific for the different STAT proteins and may function to direct selective transcriptional activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, X -- Sun, Y L -- Hoey, T -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):794-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Line ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/immunology/*metabolism ; Interferon-gamma/genetics ; Introns ; Molecular Sequence Data ; Mutation ; Oligodeoxyribonucleotides/metabolism ; Promoter Regions, Genetic ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; Sequence Deletion ; Signal Transduction ; Trans-Activators/chemistry/immunology/*metabolism ; *Transcriptional Activation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    A permease-oxidase complex involved in high-affinity iron uptake in yeast (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene--were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stearman, R -- Yuan, D S -- Yamaguchi-Iwai, Y -- Klausner, R D -- Dancis, A -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1552-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599111" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biological Transport ; Carrier Proteins/chemistry/*genetics/*metabolism ; Cell Membrane/metabolism ; *Ceruloplasmin ; Copper/metabolism/pharmacology ; Endoplasmic Reticulum/metabolism ; Ferric Compounds/metabolism ; Ferritins/chemistry/metabolism ; Ferrous Compounds/metabolism ; Genes, Fungal ; Golgi Apparatus/metabolism ; Iron/*metabolism ; Membrane Transport Proteins/chemistry/*genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Multienzyme Complexes/*metabolism ; Mutation ; Open Reading Frames ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transformation, Genetic
    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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  • 4
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    Evaluating electrostatic contributions to binding with the use of protein charge ladders (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-26
    Description: Electrostatic interactions between charges on ligands and charges on proteins that are remote from the binding interface can influence the free energy of binding (delta Gb). The binding affinities between charged ligands and the members of a charge ladder of bovine carbonic anhydrase (CAII) constructed by random acetylation of the amino groups on its surface were measured by affinity capillary electrophoresis (ACE). The values of delta Gb derived from this analysis correlated approximately linearly with the charge. Opposite charges on the ligand and the members of the charge ladder of CAII were stabilizing; like charges were destabilizing. The combination of ACE and protein charge ladders provides a tool for quantitatively examining the contributions of electrostatics to free energies of molecular recognition in biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, J -- Mammen, M -- Whitesides, G M -- GM51559/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):535-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614800" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Animals ; Binding Sites ; Carbonic Anhydrases/*chemistry/*metabolism ; Cattle ; Electrochemistry ; Electrophoresis, Capillary ; Ligands ; Models, Chemical ; Molecular Weight ; Protein Conformation ; Sulfonamides/metabolism ; Thermodynamics
    Print ISSN: 0036-8075
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  • 5
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    Crystal structure of a group I ribozyme domain: principles of RNA packing (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-20
    Description: Group I self-splicing introns catalyze their own excision from precursor RNAs by way of a two-step transesterification reaction. The catalytic core of these ribozymes is formed by two structural domains. The 2.8-angstrom crystal structure of one of these, the P4-P6 domain of the Tetrahymena thermophila intron, is described. In the 160-nucleotide domain, a sharp bend allows stacked helices of the conserved core to pack alongside helices of an adjacent region. Two specific long-range interactions clamp the two halves of the domain together: a two-Mg2+-coordinated adenosine-rich corkscrew plugs into the minor groove of a helix, and a GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal- and ribose-mediated backbone contacts further stabilize the close side-by-side helical packing. The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cate, J H -- Gooding, A R -- Podell, E -- Zhou, K -- Golden, B L -- Kundrot, C E -- Cech, T R -- Doudna, J A -- 5T32GM08283-07/GM/NIGMS NIH HHS/ -- GM22778-21/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1678-85.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. doudna@csb.yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8781224" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/chemistry ; Animals ; Base Composition ; Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Hydrogen Bonding ; *Introns ; Magnesium/chemistry ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Phosphates/chemistry ; Phylogeny ; RNA Splicing ; RNA, Catalytic/*chemistry/metabolism ; RNA, Protozoan/*chemistry/metabolism ; Ribose/chemistry ; Tetrahymena thermophila/genetics
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  • 6
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    Structure of the amino-terminal core domain of the HIV-1 capsid protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: The three-dimensional structure of the amino-terminal core domain (residues 1 through 151) of the human immunodeficiency virus-type 1 (HIV-1) capsid protein has been solved by multidimensional heteronuclear magnetic resonance spectroscopy. The structure is unlike those of previously characterized viral coat proteins and is composed of seven alpha helices, two beta hairpins, and an exposed partially ordered loop. The domain is shaped like an arrowhead, with the beta hairpins and loop exposed at the trailing edge and the carboxyl-terminal helix projecting from the tip. The proline residue Pro1 forms a salt bridge with a conserved, buried aspartate residue (Asp51), which suggests that the amino terminus of the protein rearranges upon proteolytic maturation. The binding site for cyclophilin A, a cellular rotamase that is packaged into the HIV-1 virion, is located on the exposed loop and encompasses the essential proline residue Pro90. In the free monomeric domain, Pro90 adopts kinetically trapped cis and trans conformations, raising the possibility that cyclophilin A catalyzes interconversion of the cis- and trans-Pro90 loop structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gitti, R K -- Lee, B M -- Walker, J -- Summers, M F -- Yoo, S -- Sundquist, W I -- AI30917/AI/NIAID NIH HHS/ -- CA 42014/CA/NCI NIH HHS/ -- GM 42561/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):231-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore, MD 21228, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662505" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/metabolism ; Amino Acid Sequence ; Aspartic Acid/chemistry ; Binding Sites ; Capsid/*chemistry/metabolism ; Carrier Proteins/metabolism ; HIV Core Protein p24/*chemistry/metabolism ; HIV-1/*chemistry ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Peptidylprolyl Isomerase ; Proline/chemistry ; Protein Conformation ; Protein Processing, Post-Translational ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Virion/chemistry
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  • 7
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    Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-04
    Description: Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rep, M -- van Dijl, J M -- Suda, K -- Schatz, G -- Grivell, L A -- Suzuki, C K -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cell Biology, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810243" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Dependent Proteases ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Electron Transport Complex IV/metabolism ; Fungal Proteins/*metabolism ; Heat-Shock Proteins/genetics/*metabolism ; Membrane Proteins/*metabolism ; *Metalloendopeptidases ; Mitochondria/*metabolism ; Mitochondrial Proteins ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Proton-Translocating ATPases/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*metabolism ; *Saccharomyces cerevisiae Proteins ; Serine Endopeptidases/genetics/*metabolism
    Print ISSN: 0036-8075
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  • 8
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    Catalytic role of 2'-hydroxyl groups within a group II intron active site (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: Domain 5 is an essential active-site component of group II intron ribozymes. The role of backbone substituents in D5 function was explored through synthesis of a series of derivatives containing deoxynucleotides at each position along the D5 strand. Kinetic screens revealed that eight 2'-hydroxyl groups were likely to be critical for activity of D5. Through two separate methods, including competitive inhibition and direct kinetic analysis, effects on binding and chemistry were distinguished. Depending on their function, important 2'-hydroxyl groups lie on opposite faces of the molecule, defining distinct loci for molecular recognition and catalysis by D5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abramovitz, D L -- Friedman, R A -- Pyle, A M -- GM41371/GM/NIGMS NIH HHS/ -- GM50313/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1410-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596912" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; Catalysis ; Exons ; Hydrogen Bonding ; Hydroxyl Radical/chemistry ; *Introns ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/metabolism ; RNA/metabolism ; RNA, Catalytic/chemistry/*metabolism
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  • 9
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    Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: Rapamycin, a potent immunosuppressive agent, binds two proteins: the FK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and the FKBP12-rapamycin-binding (FRB) domain of human FRAP at a resolution of 2.7 angstroms revealed the two proteins bound together as a result of the ability of rapamycin to occupy two different hydrophobic binding pockets simultaneously. The structure shows extensive interactions between rapamycin and both proteins, but fewer interactions between the proteins. The structure of the FRB domain of FRAP clarifies both rapamycin-independent and -dependent effects observed for mutants of FRAP and its homologs in the family of proteins related to the ataxia-telangiectasia mutant gene product, and it illustrates how a small cell-permeable molecule can mediate protein dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, J -- Chen, J -- Schreiber, S L -- Clardy, J -- CA59021/CA/NCI NIH HHS/ -- GM38625/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, NY 14853-1301, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662507" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carrier Proteins/chemistry/genetics/*metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/*metabolism ; Heat-Shock Proteins/chemistry/*metabolism ; Humans ; *Immunophilins ; Models, Molecular ; Mutation ; *Phosphotransferases (Alcohol Group Acceptor) ; Polyenes/*chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Sirolimus ; TOR Serine-Threonine Kinases ; Tacrolimus Binding Proteins
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  • 10
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    A mechanism of drug action revealed by structural studies of enoyl reductase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2' hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baldock, C -- Rafferty, J B -- Sedelnikova, S E -- Baker, P J -- Stuitje, A R -- Slabas, A R -- Hawkes, T R -- Rice, D W -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK. D.Rice@sheffield.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953047" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/*metabolism/pharmacology ; Binding Sites ; Boron Compounds/*metabolism/pharmacology ; Crystallography, X-Ray ; Drug Design ; Drug Resistance, Microbial ; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) ; Enzyme Inhibitors/*metabolism/pharmacology ; Escherichia coli/enzymology ; Escherichia coli Proteins ; Fatty Acid Synthase, Type II ; Fatty Acid Synthases/antagonists & inhibitors/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; NAD/*metabolism ; Oxidoreductases/antagonists & inhibitors/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary
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  • 11
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    Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Human leukocyte antigen (HLA)-DM is a critical participant in antigen presentation that catalyzes the release of class II-associated invariant chain-derived peptides (CLIP) from newly synthesized class II histocompatibility molecules, freeing the peptide-binding site for acquisition of antigenic peptides. The mechanism for the selective release of CLIP but not other peptides is unknown. DM was found to enhance the rate of peptide dissociation to an extent directly proportional to the intrinsic rate of peptide dissociation from HLA-DR, regardless of peptide sequence. Thus, CLIP is rapidly released in the presence of DM, because its intrinsic rate of dissociation is relatively high. In antigen presentation, DM has the potential to markedly enhance the rate of peptide exchange, favoring the presentation of peptides with slower intrinsic rates of dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, D A -- Evavold, B D -- Jensen, P E -- AI30554/AI/NIAID NIH HHS/ -- AI33614/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):618-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849454" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigen Presentation ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Binding Sites ; HLA-D Antigens/*metabolism ; HLA-DR Antigens/immunology/*metabolism ; Histocompatibility Antigens Class II/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Peptides/immunology/*metabolism ; Recombinant Fusion Proteins/metabolism
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  • 12
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    Identification of MAP kinase domains by redirecting stress signals into growth factor responses (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Mitogen-activated protein kinase (MAPK) cascades, termed MAPK modules, channel extracellular signals into specific cellular responses. Chimeric molecules were constructed between p38 and p44 MAPKs, which transduce stress and growth factor signals, respectively. A discrete region of 40 residues located in the amono-terminal p38MAPK lobe directed the specificity of response to extracellular signals, whereas the p44MAPK chimera, expressed in vivo, redirected stress signals into early mitogenic responses, demonstrating the functional independence of these domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brunet, A -- Pouyssegur, J -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochemie-CNRS, UMR134, Parc Valrose, Faculte des Sciences, Nice, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658140" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anisomycin/pharmacology ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; Cell Division ; Cell Line ; Cricetinae ; Cricetulus ; Enzyme Activation ; Gene Expression Regulation ; Genes, fos ; Growth Substances/metabolism ; Mice ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation/drug effects ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribosomal Protein S6 Kinases ; Signal Transduction ; Sorbitol/pharmacology ; Substrate Specificity ; p38 Mitogen-Activated Protein Kinases
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  • 13
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    Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2 (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-08
    Description: Mutations in the p53 tumor suppressor are among the most frequently observed genetic alterations in human cancer and map to the 200-amino acid core domain of the protein. The core domain contains the sequence-specific DNA binding activity and the in vitro 53BP2 protein binding activity of p53. The crystal structure of the p53 core domain bound to the 53BP2 protein, which contains an SH3 (Src homology 3) domain and four ankyrin repeats, revealed that (i) the SH3 domain binds the L3 loop of p53 in a manner distinct from that of previously characterized SH3-polyproline peptide complexes, and (ii) an ankyrin repeat, which forms an L-shaped structure consisting of a beta hairpin and two alpha helices, binds the L2 loop of p53. The structure of the complex shows that the 53BP2 binding site on the p53 core domain consists of evolutionarily conserved regions that are frequently mutated in cancer and that it overlaps the site of DNA binding. The six most frequently observed p53 mutations disrupt 53BP2 binding in vitro. The structure provides evidence that the 53BP2-p53 complex forms in vivo and may have a critical role in the p53 pathway of tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorina, S -- Pavletich, N P -- CA65698/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):1001-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875926" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ankyrins/*chemistry ; Apoptosis Regulatory Proteins ; Binding Sites ; Carrier Proteins/*chemistry/metabolism ; Crystallography, X-Ray ; DNA/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neoplasms/genetics ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism ; *src Homology Domains
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  • 14
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    Iron metabolism in eukaryotes: Mars and Venus at it again (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaplan, J -- O'Halloran, T V -- R01 GM038784/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1510-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Utah School of Medicine, Salt Lake City, 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599104" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biological Transport ; Carrier Proteins/genetics/*metabolism ; Ceruloplasmin/chemistry/*metabolism ; Copper/metabolism ; Ferric Compounds/metabolism ; Ferrous Compounds/metabolism ; Iron/*metabolism ; Membrane Transport Proteins/genetics/*metabolism ; Models, Molecular ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Protein Conformation ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins
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  • 15
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    Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-01-12
    Description: Cations bind to the pi face of an aromatic structure through a surprisingly strong, non-covalent force termed the cation-pi interaction. The magnitude and generality of the effect have been established by gas-phase measurements and by studies of model receptors in aqueous media. To first order, the interaction can be considered an electrostatic attraction between a positive charge and the quadrupole moment of the aromatic. A great deal of direct and circumstantial evidence indicates that cation-pi interactions are important in a variety of proteins that bind cationic ligands or substrates. In this context, the amino acids phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) can be viewed as polar, yet hydrophobic, residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dougherty, D A -- GM43936/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):163-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539615" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Benzene/chemistry/*metabolism ; Binding Sites ; Cations/chemistry/*metabolism ; Chemistry, Physical ; Ion Channels/metabolism ; Phenylalanine/chemistry/*metabolism ; Physicochemical Phenomena ; Proteins/*metabolism ; Receptors, Cholinergic/metabolism ; Steroids/biosynthesis ; Tryptophan/chemistry/*metabolism ; Tyrosine/chemistry/*metabolism ; Water/chemistry/metabolism
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  • 16
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    Change of a catalytic reaction carried out by a DNA replication protein (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-01
    Description: The RepA protein of plasmid pC194 initiates and terminates rolling circle replication. At initiation, it forms a 5'-phosphotyrosyl DNA link, whereas at termination, a glutamate residue directs hydrolytic cleavage of the newly synthesized origin, and the resulting 3'-hydroxyl group undergoes transesterification with the phosphotyrosine link. The protein is thus released from DNA, and the termination is uncoupled from reinitiation of replication. Replacement of the glutamate with tyrosine in RepA altered this mechanism, so that termination occurred by two successive transesterifications and became coupled to reinitiation. This result suggests that various enzymes involved in DNA cleavage and rejoining may have similar mechanistic and evolutionary roots.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noirot-Gros, M F -- Ehrlich, S D -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):777-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetique Microbienne, Institut National de la Recherche Agronomique, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864116" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage phi X 174 ; Binding Sites ; *DNA Helicases ; *DNA Replication ; DNA, Bacterial/*metabolism ; DNA, Single-Stranded/metabolism ; DNA, Viral/metabolism ; *DNA-Binding Proteins ; Esterification ; Evolution, Molecular ; Glutamic Acid/metabolism ; Hydrolysis ; Mutation ; Plasmids ; Proteins/chemistry/genetics/*metabolism ; *Trans-Activators ; Tyrosine/metabolism ; Viral Proteins/metabolism
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  • 17
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    Homologous DNA pairing promoted by a 20-amino acid peptide derived from RecA (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-10
    Description: The molecular structure of the Escherichia coli RecA protein in the absence of DNA revealed two disordered or mobile loops that were proposed to be DNA binding sites. A short peptide spanning one of these loops was shown to carry out the key reaction mediated by the whole RecA protein: pairing (targeting) of a single-stranded DNA to its homologous site on a duplex DNA. In the course of the reaction the peptide bound to both substrate DNAs, unstacked the single-stranded DNA, and assumed a beta structure. These events probably recapitulate the underlying molecular pathway or mechanism used by homologous recombination proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Voloshin, O N -- Wang, L -- Camerini-Otero, R D -- New York, N.Y. -- Science. 1996 May 10;272(5263):868-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-1810, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629021" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA, Single-Stranded/chemistry/genetics/*metabolism ; DNA, Superhelical/chemistry/genetics/*metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Peptide Fragments/chemistry/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Rec A Recombinases/chemistry/*metabolism ; *Recombination, Genetic
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  • 18
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    Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-06-14
    Description: The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been implicated in cloud nucleation and global climate regulation. The crystal structure of DMSO reductase from Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states. The change in pterin coordination between the Mo(VI) and Mo(IV) forms suggests a mechanism for substrate binding and reduction by this enzyme. Sequence comparisons of DMSO reductase with a family of bacterial oxotransferases containing molybdopterin guanine dinucleotide indicate a similar polypeptide fold and active site with two molybdopterins within this family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schindelin, H -- Kisker, C -- Hilton, J -- Rajagopalan, K V -- Rees, D C -- GM00091/GM/NIGMS NIH HHS/ -- GM50775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1615-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658134" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Coenzymes/*chemistry ; Crystallography, X-Ray ; *Iron-Sulfur Proteins ; Metalloproteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/*chemistry/metabolism ; Protein Conformation ; Pteridines/*chemistry ; Rhodobacter sphaeroides/*enzymology ; Sequence Homology, Amino Acid
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  • 19
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    Crystal structure of the lactose operon repressor and its complexes with DNA and inducer (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-03-01
    Description: The lac operon of Escherichia coli is the paradigm for gene regulation. Its key component is the lac repressor, a product of the lacI gene. The three-dimensional structures of the intact lac repressor, the lac repressor bound to the gratuitous inducer isopropyl-beta-D-1-thiogalactoside (IPTG) and the lac repressor complexed with a 21-base pair symmetric operator DNA have been determined. These three structures show the conformation of the molecule in both the induced and repressed states and provide a framework for understanding a wealth of biochemical and genetic information. The DNA sequence of the lac operon has three lac repressor recognition sites in a stretch of 500 base pairs. The crystallographic structure of the complex with DNA suggests that the tetrameric repressor functions synergistically with catabolite gene activator protein (CAP) and participates in the quaternary formation of repression loops in which one tetrameric repressor interacts simultaneously with two sites on the genomic DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewis, M -- Chang, G -- Horton, N C -- Kercher, M A -- Pace, H C -- Schumacher, M A -- Brennan, R G -- Lu, P -- 2-T32-GM082745/GM/NIGMS NIH HHS/ -- GM44617/GM/NIGMS NIH HHS/ -- P41-RR06017/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1247-54.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johnson Research Foundation, University of Pennsylvania, Philadelphia 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638105" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Bacterial Proteins/*chemistry/genetics/metabolism ; Base Sequence ; Binding Sites ; Crystallography, X-Ray ; Cyclic AMP Receptor Protein/metabolism ; DNA, Bacterial/chemistry/*metabolism ; *Escherichia coli Proteins ; Hydrogen Bonding ; Isopropyl Thiogalactoside/*metabolism ; *Lac Operon ; Lac Repressors ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Operator Regions, Genetic ; Point Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Repressor Proteins/*chemistry/genetics/metabolism
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  • 20
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    The galvanization of biology: a growing appreciation for the roles of zinc (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-02-23
    Description: Zinc ions are key structural components of a large number of proteins. The binding of zinc stabilizes the folded conformations of domains so that they may facilitate interactions between the proteins and other macromolecules such as DNA. The modular nature of some of these zinc-containing proteins has allowed the rational design of site-specific DNA binding proteins. The ability of zinc to be bound specifically within a range of tetrahedral sites appears to be responsible for the evolution of the side range of zinc-stabilized structural domains now known to exist. The lack of redox activity for the zinc ion and its binding and exchange kinetics also may be important in the use of zinc for specific functional roles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, J M -- Shi, Y -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1081-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599083" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Engineering ; Transcription Factors/chemistry/*metabolism ; Zinc/chemistry/metabolism/*physiology ; Zinc Fingers/*physiology
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  • 21
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    Identification of D-peptide ligands through mirror-image phage display (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-03-29
    Description: Genetically encoded libraries of peptides and oligonucleotides are well suited for the identification of ligands for many macromolecules. A major drawback of these techniques is that the resultant ligands are subject to degradation by naturally occurring enzymes. Here, a method is described that uses a biologically encoded library for the identification of D-peptide ligands, which should be resistant to proteolytic degradation. In this approach, a protein is synthesized in the D-amino acid configuration and used to select peptides from a phage display library expressing random L-amino acid peptides. For reasons of symmetry, the mirror images of these phage-displayed peptides interact with the target protein of the natural handedness. The value of this approach was demonstrated by the identification of a cyclic D-peptide that interacts with the Src homology 3 domain of c- SRC. Nuclear magnetic resonance studies indicate that the binding site for this D-peptide partially overlaps the site for the physiological ligands of this domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schumacher, T N -- Mayr, L M -- Minor, D L Jr -- Milhollen, M A -- Burgess, M W -- Kim, P S -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1854-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596952" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages ; Base Sequence ; Binding Sites ; Chickens ; Cloning, Molecular ; Gene Library ; Ligands ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Peptides/chemistry/genetics/*metabolism ; Peptides, Cyclic/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins pp60(c-src)/chemistry/*metabolism ; Stereoisomerism ; *src Homology Domains
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  • 22
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    A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-08-23
    Description: A previously unknown redox cofactor has been identified in the active site of lysyl oxidase from the bovine aorta. Edman sequencing, mass spectrometry, ultraviolet-visible spectra, and resonance Raman studies showed that this cofactor is a quinone. Its structure is derived from the crosslinking of the epsilon-amino group of a peptidyl lysine with the modified side chain of a tyrosyl residue, and it has been designated lysine tyrosylquinone. This quinone appears to be the only example of a mammalian cofactor formed from the crosslinking of two amino acid side chains. This discovery expands the range of known quino-cofactor structures and has implications for the mechanism of their biogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, S X -- Mure, M -- Medzihradszky, K F -- Burlingame, A L -- Brown, D E -- Dooley, D M -- Smith, A J -- Kagan, H M -- Klinman, J P -- GM27659/GM/NIGMS NIH HHS/ -- GM39296/GM/NIGMS NIH HHS/ -- P41 RR01614/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1078-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688089" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aorta/enzymology ; Binding Sites ; Cattle ; Chromatography, High Pressure Liquid ; Lysine/*analogs & derivatives/chemistry/metabolism ; Mass Spectrometry ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Protein-Lysine 6-Oxidase/*chemistry/genetics/isolation & purification/metabolism ; Quinones/*chemistry/metabolism ; Spectrophotometry, Ultraviolet ; Spectrum Analysis, Raman
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  • 23
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    Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-01-26
    Description: A subset of individuals with familial amyotrophic lateral sclerosis (FALS) possesses dominantly inherited mutations in the gene that encodes copper-zinc superoxide dismutase (CuZnSOD). A4V and G93A, two of the mutant enzymes associated with FALS, were shown to catalyze the oxidation of a model substrate (spin trap 5,5'-dimethyl-1-pyrroline N-oxide) by hydrogen peroxide at a higher rate than that seen with the wild-type enzyme. Catalysis of this reaction by A4V and G93A was more sensitive to inhibition by the copper chelators diethyldithiocarbamate and penicillamine than was catalysis by wild-type CuZnSOD. The same two chelators reversed the apoptosis-inducing effect of mutant enzymes expressed in a neural cell line. These results suggest that oxidative reactions catalyzed by mutant CuZnSOD enzymes initiate the neuropathologic changes in FALS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wiedau-Pazos, M -- Goto, J J -- Rabizadeh, S -- Gralla, E B -- Roe, J A -- Lee, M K -- Valentine, J S -- Bredesen, D E -- AG12282/AG/NIA NIH HHS/ -- DK46828/DK/NIDDK NIH HHS/ -- GM28222/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):515-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560268" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*enzymology/genetics ; Animals ; Apoptosis/drug effects ; Binding Sites ; Catalysis ; Cell Line ; Chelating Agents/pharmacology ; Copper/metabolism ; Cyclic N-Oxides/metabolism ; Ditiocarb/pharmacology ; Humans ; Hydrogen Peroxide/metabolism ; Mutation ; Oxidation-Reduction ; Penicillamine/pharmacology ; Rats ; Superoxide Dismutase/genetics/*metabolism
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  • 24
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    Antibacterial agents that inhibit lipid A biosynthesis (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-08
    Description: Lipid A constitutes the outer monolayer of the outer membrane of Gram-negative bacteria and is essential for bacterial growth. Synthetic antibacterials were identified that inhibit the second enzyme (a unique deacetylase) of lipid A biosynthesis. The inhibitors are chiral hydroxamic acids bearing certain hydrophobic aromatic moieties. They may bind to a metal in the active site of the deacetylase. The most potent analog (with an inhibition constant of about 50 nM) displayed a minimal inhibitory concentration of about 1 microgram per milliliter against Escherichia coli, caused three logs of bacterial killing in 4 hours, and cured mice infected with a lethal intraperitoneal dose of E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onishi, H R -- Pelak, B A -- Gerckens, L S -- Silver, L L -- Kahan, F M -- Chen, M H -- Patchett, A A -- Galloway, S M -- Hyland, S A -- Anderson, M S -- Raetz, C R -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):980-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Merck Research Laboratories, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875939" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/*antagonists & inhibitors/metabolism ; Animals ; Anti-Bacterial Agents/chemistry/*pharmacology ; Binding Sites ; Escherichia coli/drug effects ; Escherichia coli Infections/drug therapy ; Gram-Negative Bacteria/*drug effects ; Hydroxamic Acids/chemistry/*pharmacology ; Lipid A/*biosynthesis ; Mice ; Microbial Sensitivity Tests ; Oxazoles/chemistry/pharmacology ; Pseudomonas/drug effects ; Serratia/drug effects ; Stereoisomerism ; Structure-Activity Relationship
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  • 25
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    Structural analysis of substrate binding by the molecular chaperone DnaK (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 angstroms resolution. The structure consists of a beta-sandwich subdomain followed by alpha-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the beta sandwich. An alpha-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, X -- Zhao, X -- Burkholder, W F -- Gragerov, A -- Ogata, C M -- Gottesman, M E -- Hendrickson, W A -- GM 34102/GM/NIGMS NIH HHS/ -- GM 37219/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1606-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658133" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Chaperonins/chemistry/*metabolism ; Crystallography, X-Ray ; Escherichia coli ; *Escherichia coli Proteins ; HSP70 Heat-Shock Proteins/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptides/metabolism ; Protein Binding ; Protein Conformation ; Sequence Homology, Amino Acid
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    Direct visualization of A-, P-, and E-site transfer RNAs in the Escherichia coli ribosome (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: Transfer RNA (tRNA) molecules play a crucial role in protein biosynthesis in all organisms. Their interactions with ribosomes mediate the translation of genetic messages into polypeptides. Three tRNAs bound to the Escherichia coli 70S ribosome were visualized directly with cryoelectron microscopy and three-dimensional reconstruction. The detailed arrangement of A- and P-site tRNAs inferred from this study allows localization of the sites for anticodon interaction and peptide bond formation on the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agrawal, R K -- Penczek, P -- Grassucci, R A -- Li, Y -- Leith, A -- Nierhaus, K H -- Frank, J -- 1R01 GM29169/GM/NIGMS NIH HHS/ -- P41 RR01219/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):1000-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wadsworth Center, New York State Department of Health, Albany 12201-0509, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584922" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon ; Binding Sites ; Codon ; Escherichia coli/*metabolism ; Image Processing, Computer-Assisted ; Microscopy, Electron ; Models, Molecular ; Nucleic Acid Conformation ; RNA, Bacterial/chemistry/metabolism ; RNA, Transfer/*chemistry/metabolism ; RNA, Transfer, Amino Acyl/*chemistry/metabolism ; RNA, Transfer, Phe/*chemistry/metabolism ; Ribosomes/*metabolism
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    Angiotensin II-forming activity in a reconstructed ancestral chymase (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-01-26
    Description: The current model of serine protease diversity theorizes that the earliest protease molecules were simple digestive enzymes that gained complex regulatory functions and restricted substrate specificities through evolution. Among the chymase group of serine proteases are enzymes that convert angiotensin I to angiotensin II, as well as others that simply degrade angiotensins. An ancestral chymase reconstructed with the use of phylogenetic inference, total gene synthesis, and protein expression had efficient and specific angiotensin II-forming activity (turnover number, about 700 per second). Thus, angiotensin II-forming activity is the more primitive state for chymases, and the loss of such activity occurred later in the evolution of some of these serine proteases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandrasekharan, U M -- Sanker, S -- Glynias, M J -- Karnik, S S -- Husain, A -- HL33713/HL/NHLBI NIH HHS/ -- HL44201/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):502-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cardiology, Cleveland Clinic Foundation, OH 44195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560264" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiotensin I/*metabolism ; Angiotensin II/*metabolism ; Angiotensins/metabolism ; Animals ; Binding Sites ; Chymases ; Evolution, Molecular ; Genes, Synthetic ; Humans ; Molecular Sequence Data ; Rats ; Serine Endopeptidases/chemistry/genetics/*metabolism ; Substrate Specificity
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    Crystal structure of the dual specificity protein phosphatase VHR (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. Here, the crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1 angstrom resolution. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region," connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuvaniyama, J -- Denu, J M -- Dixon, J E -- Saper, M A -- AI 34095/AI/NIAID NIH HHS/ -- DK18024/DK/NIDDK NIH HHS/ -- DK18849/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 May 31;272(5266):1328-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysics Research Division and Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-1055, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650541" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Dual Specificity Phosphatase 3 ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Phosphotyrosine/metabolism ; *Protein Conformation ; Protein Folding ; *Protein Structure, Secondary ; Protein Tyrosine Phosphatases/*chemistry/metabolism ; Sequence Alignment ; Substrate Specificity ; Water/metabolism ; Yersinia/enzymology
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    An asymmetric model for the nucleosome: a binding site for linker histones inside the DNA gyres (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-10-25
    Description: Histone-DNA contacts within a nucleosome influence the function of trans-acting factors and the molecular machines required to activate the transcription process. The internal architecture of a positioned nucleosome has now been probed with the use of photoactivatable cross-linking reagents to determine the placement of histones along the DNA molecule. A model for the nucleosome is proposed in which the winged-helix domain of the linker histone is asymmetrically located inside the gyres of DNA that also wrap around the core histones. This domain extends the path of the protein superhelix to one side of the core particle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pruss, D -- Bartholomew, B -- Persinger, J -- Hayes, J -- Arents, G -- Moudrianakis, E N -- Wolffe, A P -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):614-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2710, USA. awlme@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849453" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cross-Linking Reagents ; DNA/*chemistry/metabolism ; Histones/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleosomes/*chemistry ; Protein Conformation ; Protein Structure, Secondary ; RNA, Ribosomal/genetics ; Recombinant Proteins/chemistry ; Xenopus
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    Mapping of catalytic residues in the RNA polymerase active center (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-07-05
    Description: When the Mg2+ ion in the catalytic center of Escherichia coli RNA polymerase (RNAP) is replaced with Fe2+, hydroxyl radicals are generated. In the promoter complex, such radicals cleave template DNA near the transcription start site, whereas the beta' subunit is cleaved at a conserved motif NADFDGD (Asn-Ala-Asp-Phe-Asp-Gly-Asp). Substitution of the three aspartate residues with alanine creates a dominant lethal mutation. The mutant RNAP is catalytically inactive but can bind promoters and form an open complex. The mutant fails to support Fe2+-induced cleavage of DNA or protein. Thus, the NAD-FDGD motif is involved in chelation of the active center Mg2+.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaychikov, E -- Martin, E -- Denissova, L -- Kozlov, M -- Markovtsov, V -- Kashlev, M -- Heumann, H -- Nikiforov, V -- Goldfarb, A -- Mustaev, A -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):107-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Limnological Institute, Russian Academy of Sciences, Irkutsk, Russia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658176" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; DNA/metabolism ; DNA-Directed RNA Polymerases/*chemistry/genetics/*metabolism ; Dithiothreitol/pharmacology ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*enzymology ; Ferrous Compounds/metabolism ; Hydroxyl Radical ; Magnesium/metabolism ; Molecular Sequence Data ; Mutagenesis ; Promoter Regions, Genetic
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    Cell growth arrest and induction of cyclin-dependent kinase inhibitor p21 WAF1/CIP1 mediated by STAT1 (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-05-03
    Description: Signal transducers and activators of transcription (STAT) proteins can be conditionally activated in response to epidermal growth factor (EGF) and interferon (IFN)-gamma. STAT activation was correlated with cell growth inhibition in response to EGF and IFN-gamma. Activated STAT proteins specifically recognized the conserved STAT-responsive elements in the promoter of the gene encoding the cyclin-dependent kinase (CDK) inhibitor p21 WAF1/CIP1 and regulated the induction of p21 messenger RNA. IFN-gamma did not inhibit the growth of U3A cells, which are deficient in STAT1, but did inhibit the growth of U3A cells into which STAT1 alpha was reintroduced. Thus, STAT1 protein is essential for cell growth suppression in response to IFN-gamma. The STAT signaling pathway appears to negatively regulate the cell cycle by inducing CDK inhibitors in response to cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chin, Y E -- Kitagawa, M -- Su, W C -- You, Z H -- Iwamoto, Y -- Fu, X Y -- R01 AI34522/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 May 3;272(5262):719-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Yale University School of Medicine, New Haven, CT 06520-8023, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614832" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; *Cell Division/drug effects ; Cell Line ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins/biosynthesis/*genetics ; DNA/biosynthesis ; DNA-Binding Proteins/metabolism/*physiology ; Epidermal Growth Factor/pharmacology ; *Gene Expression Regulation ; Humans ; Interferon-gamma/pharmacology ; Molecular Sequence Data ; Promoter Regions, Genetic ; RNA, Messenger/genetics/metabolism ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/metabolism/*physiology ; Transfection ; Tumor Cells, Cultured
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    Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-08
    Description: The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kussie, P H -- Gorina, S -- Marechal, V -- Elenbaas, B -- Moreau, J -- Levine, A J -- Pavletich, N P -- CA65698/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):948-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA. nikola@xray2.mskcc.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875929" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; *Nuclear Proteins ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/*chemistry/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Transcription Factors/chemistry/metabolism ; *Transcriptional Activation ; Tumor Suppressor Protein p53/*chemistry/metabolism
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    Targeting of motor proteins (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-03-15
    Description: Microtubules are responsible for chromosome segregation and the movement and reorganization of membranous organelles. Many aspects of microtubule-based motility can be attributed to the action of motor proteins, producing force directed toward either end of microtubules. How these proteins are targeted to the appropriate organellar sites within the cell, however, has remained a mystery. Recent work has begun to define the targeting mechanism for two well-studied motor proteins, kinesin and cytoplasmic dynein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vallee, R B -- Sheetz, M P -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1539-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Worcester Foundation for Biomedical Research, Shrewsbury, MA 01545, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599110" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biological Transport ; Cytoplasm/metabolism ; Dyneins/chemistry/*metabolism ; Intracellular Membranes/*metabolism ; Kinesin/chemistry/*metabolism ; *Membrane Proteins ; Microtubule Proteins/metabolism ; *Microtubule-Associated Proteins ; Microtubules/*physiology ; Models, Biological ; Organelles/*metabolism ; Receptors, Cell Surface/chemistry/metabolism
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    Flexing muscle with just one amino acid (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539593" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Calcium/*metabolism ; Glutamic Acid/*physiology ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; *Muscle Contraction ; Muscle, Skeletal/chemistry ; Mutation ; Myocardium/chemistry ; *Protein Conformation ; Protein Structure, Secondary ; Troponin/*chemistry/genetics/metabolism ; Troponin C
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    Linker histones, DNA's protein custodians, gain new respect (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):503-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8928004" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; Gene Expression Regulation ; Histones/chemistry/*metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Nucleosomes/*chemistry/genetics ; Tetrahymena thermophila/genetics ; Xenopus
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    Filling in the blanks in the p53 protein structure (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-11-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):921-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966571" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis Regulatory Proteins ; Binding Sites ; Carrier Proteins/*chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; DNA/metabolism ; Magnetic Resonance Spectroscopy ; *Nuclear Proteins ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proto-Oncogene Proteins/*chemistry/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Tumor Suppressor Protein p53/*chemistry/metabolism
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    Closing in on a stomach-sparing aspirin substitute (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1996 Sep 20;273(5282):1660.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8830410" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Inflammatory Agents, Non-Steroidal/metabolism/*pharmacology ; Aspirin/*analogs & derivatives/metabolism/pharmacology ; Binding Sites ; Cyclooxygenase 1 ; Cyclooxygenase 2 ; Cyclooxygenase 2 Inhibitors ; Cyclooxygenase Inhibitors/metabolism/*pharmacology ; Drug Design ; Humans ; Isoenzymes/chemistry/*metabolism ; Membrane Proteins ; Prostaglandin-Endoperoxide Synthases/chemistry/*metabolism
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    Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-07-26
    Description: The functional mimicry of a protein by an unrelated small molecule has been a formidable challenge. Now, however, the biological activity of a 166-residue hematopoietic growth hormone, erythropoietin (EPO), with its class 1 cytokine receptor has been mimicked by a 20-residue cyclic peptide unrelated in sequence to the natural ligand. The crystal structure at 2.8 A resolution of a complex of this agonist peptide with the extracellular domain of EPO receptor reveals that a peptide dimer induces an almost perfect twofold dimerization of the receptor. The dimer assembly differs from that of the human growth hormone (hGH) receptor complex and suggests that more than one mode of dimerization may be able to induce signal transduction and cell proliferation. The EPO receptor binding site, defined by peptide interaction, corresponds to the smaller functional epitope identified for hGH receptor. Similarly, the EPO mimetic peptide ligand can be considered as a minimal hormone, and suggests the design of nonpeptidic small molecule mimetics for EPO and other cytokines may indeed be achievable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Livnah, O -- Stura, E A -- Johnson, D L -- Middleton, S A -- Mulcahy, L S -- Wrighton, N C -- Dower, W J -- Jolliffe, L K -- Wilson, I A -- GM-49497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):464-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10666 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/8662530" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Drug Design ; Erythropoietin/*chemistry/*metabolism ; Growth Hormone/chemistry/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; *Molecular Mimicry ; Molecular Sequence Data ; Peptides, Cyclic/*chemistry/*metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Erythropoietin/*agonists/chemistry/metabolism ; Receptors, Somatotropin/chemistry/metabolism
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    Heparin structure and interactions with basic fibroblast growth factor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: Crystal structures of heparin-derived tetra- and hexasaccharides complexed with basic fibroblast growth factor (bFGF) were determined at resolutions of 1.9 and 2.2 angstroms, respectively. The heparin structure may be approximated as a helical polymer with a disaccharide rotation of 174 degrees and a translation of 8.6 angstroms along the helix axis. Both molecules bound similarly to a region of the bFGF surface containing residues asparagine-28, arginine-121, lysine-126, and glutamine-135, the hexasaccharide also interacted with an additional binding site formed by lysine-27, asparagine-102, and lysine-136. No significant conformational change in bFGF occurred upon heparin oligosaccharide binding, which suggests that heparin primarily serves to juxtapose components of the FGF signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Faham, S -- Hileman, R E -- Fromm, J R -- Linhardt, R J -- Rees, D C -- GM38060/GM/NIGMS NIH HHS/ -- GM45162/GM/NIGMS NIH HHS/ -- T32 GM08346/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1116-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599088" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbohydrate Conformation ; Carbohydrate Sequence ; Crystallization ; Crystallography, X-Ray ; Fibroblast Growth Factor 2/*metabolism ; Heparin/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides/chemistry/metabolism ; Protein Conformation
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    Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-18
    Description: Signal transduction across cell membranes often involves interactions among identical receptor subunits, but the contribution of individual subunits is not well understood. The chemoreceptors of enteric bacteria mediate attractant responses by interrupting a phosphotransfer circuit initiated at receptor complexes with the protein kinase CheA. The aspartate receptor (Tar) is a homodimer, and oligomerized cytoplasmic domains stimulate CheA activity much more than monomers do in vitro. Intragenic complementation was used to show in Escherichia coli that heterodimers containing one full-length and one truncated Tar subunit mediated responses to aspartate in the presence of full-length Tar homodimers that could not bind aspartate. Thus, a Tar dimer containing only one cytoplasmic domain can initiate an attractant (inhibitory) signal, although it may not be able to stimulate kinase activity of CheA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardina, P J -- Manson, M D -- GM39736/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):425-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Texas A&M University, College Station, TX 77840, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8832892" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/*metabolism/pharmacology ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Chemoreceptor Cells ; Chemotaxis ; Cytoplasm/metabolism ; Dimerization ; Escherichia coli/genetics/*metabolism/physiology ; *Escherichia coli Proteins ; Genetic Complementation Test ; Membrane Proteins/chemistry/genetics/*metabolism ; Mutation ; Plasmids ; Protein Conformation ; Protein Kinases/metabolism ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Signal Transduction/*physiology
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    Signaling across membranes: a one and a two and a (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, J -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):370-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. jstock@watson.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927993" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Catalysis ; Chemoreceptor Cells ; Dimerization ; *Escherichia coli Proteins ; Humans ; Ligands ; Membrane Proteins/chemistry/genetics/*metabolism ; Protein Kinases/metabolism ; Receptors, Cell Surface/chemistry/*metabolism ; Receptors, Somatotropin/chemistry/metabolism ; Signal Transduction/*physiology
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  • 42
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    Egr-1-induced endothelial gene expression: a common theme in vascular injury (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: A number of pathophysiologically relevant genes, including platelet-derived growth factor B-chain (PDGF-B), are induced in the vasculature after acute mechanical injury. In rat aorta, the activated expression of these genes was preceded by a marked increase in the amount of the early-growth-response gene product Egr-1 at the endothelial wound edge. Egr-1 interacts with a novel element in the proximal PDGF-B promoter, as well as with consensus elements in the promoters of other genes induced by endothelial injury. This interaction is crucial for injury-induced PDGF-B promoter-dependent expression. Sp1, whose binding site in the PDGF-B promoter overlaps that of Egr-1, occupies this element in unstimulated cells and is displaced by increasing amounts of Egr-1. These findings implicate Egr-1 in the up-regulated expression of PDGF-B and other potent mediators in mechanically injured arterial endothelial cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khachigian, L M -- Lindner, V -- Williams, A J -- Collins, T -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1427-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/injuries/metabolism ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/genetics/*metabolism ; Early Growth Response Protein 1 ; Endothelium, Vascular/injuries/*metabolism ; *Gene Expression Regulation ; Genes, Reporter ; Humans ; *Immediate-Early Proteins ; Male ; Molecular Sequence Data ; Platelet-Derived Growth Factor/biosynthesis/*genetics ; *Promoter Regions, Genetic ; Rats ; Rats, Sprague-Dawley ; Recombinant Proteins/metabolism ; Sp1 Transcription Factor/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factors/genetics/*metabolism ; *Zinc Fingers
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    The whole lactose repressor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matthews, K S -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1245-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77251, USA. ksm@bioc.vice.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638104" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Bacterial Proteins/*chemistry/genetics/metabolism ; Binding Sites ; Crystallography, X-Ray ; DNA, Bacterial/metabolism ; *Escherichia coli Proteins ; Isopropyl Thiogalactoside/metabolism ; Lac Operon ; Lac Repressors ; Ligands ; Mutagenesis ; Operator Regions, Genetic ; Protein Conformation ; Protein Folding ; Repressor Proteins/*chemistry/genetics/metabolism
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  • 44
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    Mechanism of suppression of cell-mediated immunity by measles virus (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: The mechanisms underlying the profound suppression of cell-mediated immunity (CMI) accompanying measles are unclear. Interleukin-12 (IL-12), derived principally from monocytes and macrophages, is critical for the generation of CMI. Measles virus (MV) infection of primary human monocytes specifically down-regulated IL-12 production. Cross-linking of CD46, a complement regulatory protein that is the cellular receptor for MV, with antibody or with the complement activation product C3b similarly inhibited monocyte IL-12 production, providing a plausible mechanism for MV-induced immunosuppression. CD46 provides a regulatory link between the complement system and cellular immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karp, C L -- Wysocka, M -- Wahl, L M -- Ahearn, J M -- Cuomo, P J -- Sherry, B -- Trinchieri, G -- Griffin, D E -- AI01223/AI/NIAID NIH HHS/ -- AI23047/AI/NIAID NIH HHS/ -- AI35149/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):228-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662504" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Antigens, CD/immunology/*physiology ; Antigens, CD46 ; Binding Sites ; Cells, Cultured ; Chemokines/biosynthesis ; Complement C3b/immunology/physiology ; Cytokines/biosynthesis ; Down-Regulation ; Humans ; *Immune Tolerance ; Interleukin-10/physiology ; Interleukin-12/*biosynthesis ; Measles virus/*immunology/metabolism ; Membrane Glycoproteins/immunology/*physiology ; Monocytes/*immunology/*virology ; Receptors, Virus/immunology/*physiology
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  • 45
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    The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I) (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: The transition metal ion copper(II) has a critical role in chronic neurologic diseases. The amyloid precursor protein (APP) of Alzheimer's disease or a synthetic peptide representing its copper-binding site reduced bound copper(II) to copper(I). This copper ion-mediated redox reaction led to disulfide bond formation in APP, which indicated that free sulfhydryl groups of APP were involved. Neither superoxide nor hydrogen peroxide had an effect on the kinetics of copper(II) reduction. The reduction of copper(II) to copper(I) by APP involves an electron-transfer reaction and could enhance the production of hydroxyl radicals, which could then attack nearby sites. Thus, copper-mediated toxicity may contribute to neurodegeneration in Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Multhaup, G -- Schlicksupp, A -- Hesse, L -- Beher, D -- Ruppert, T -- Masters, C L -- Beyreuther, K -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1406-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ZMBH-Center for Molecular Biology Heidelberg, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596911" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amyloid beta-Protein Precursor/antagonists & inhibitors/chemistry/*metabolism ; Binding Sites ; Copper/*metabolism ; Cysteine/chemistry ; Cystine/metabolism ; Electron Transport ; Ferric Compounds/metabolism ; Histidine/chemistry ; Humans ; Hydrogen Peroxide/metabolism ; Hydroxyl Radical/metabolism ; Mass Spectrometry ; Oligopeptides/pharmacology ; Oxidation-Reduction ; Peptide Fragments/chemistry/metabolism ; Recombinant Fusion Proteins/metabolism ; Superoxides/metabolism
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  • 46
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    Use-dependent blockers and exit rate of the last ion from the multi-ion pore of a K+ channel (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: Quaternary ammonium blockers inhibit many voltage-activated potassium (K+) channels from the intracellular side. When applied to Drosophila Shaker potassium channels expressed in mammalian cells, these rapidly reversible blockers produced use-dependent inhibition through an unusual mechanism--they promoted an intrinsic conformational change known as C-type inactivation, from which recovery is slow. The blockers did so by cutting off potassium ion flow to a site in the pore, which then emptied at a rate of 10(5) ions per second. This slow rate probably reflected the departure of the last ion from the multi-ion pore: Permeation of ions (at 10(7) per second) occurs rapidly because of ion-ion repulsion, but the last ion to leave would experience no such repulsion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baukrowitz, T -- Yellen, G -- NS29693/NS/NINDS NIH HHS/ -- R01 NS029693/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):653-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School and Massachusetts General Hospital, Boston 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571129" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cell Line ; Humans ; Lidocaine/analogs & derivatives/metabolism/pharmacology ; Potassium/*metabolism ; *Potassium Channel Blockers ; Potassium Channels/metabolism ; Quaternary Ammonium Compounds/metabolism/*pharmacology ; Shaker Superfamily of Potassium Channels ; Tetraethylammonium Compounds/metabolism/pharmacology
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    Mammalian cytochrome c oxidase, a molecular monster subdued (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson-Miller, S -- New York, N.Y. -- Science. 1996 May 24;272(5265):1125.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Michigan State University, East Lansing, MI 48824-1319, USA. fergus20@pilot.msu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638156" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cattle ; Electron Transport Complex IV/*chemistry/metabolism ; Molecular Weight ; Protein Conformation ; Protons ; X-Ray Diffraction
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    The immunological evolution of catalysis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: The germline genes used by the mouse to generate the esterolytic antibody 48G7 were cloned and expressed in an effort to increase our understanding of the detailed molecular mechanisms by which the immune system evolves catalytic function. The nine replacement mutations that were fixed during affinity maturation increased affinity for the transition state analogue by a factor of 10(4), primarily the result of a decrease in the dissociation rate of the hapten-antibody complex. There was a corresponding increase in the rate of reaction of antibody with substrate, k(cat)/k(m), from 1.7 x 10(2)M(-1) min(-1) to 1.4 x 10(4)M(-1) min(-1). The three-dimensional crystal structure of the 48G7-transition state analogue complex at 2.0 angstroms resolution indicates that one of the nine residues in which somatic mutations have been fixed directly contact the hapten. Thus, in the case of 48G7, affinity maturation appears to play a conformational role, either in reorganizing the active site geometry of limiting side-chain and backbone flexibility of the germline antibody. The crystal structure and analysis of somatic and directed active site mutants underscore the role of transition state stabilization in the evolution of this catalytic antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patten, P A -- Gray, N S -- Yang, P L -- Marks, C B -- Wedemayer, G J -- Boniface, J J -- Stevens, R C -- Schultz, P G -- R01 AL24695/PHS HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1086-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599084" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Catalytic/chemistry/genetics/*immunology/metabolism ; Antibody Affinity ; Antigen-Antibody Complex ; Antigen-Antibody Reactions ; Base Sequence ; Binding Sites ; Catalysis ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; *Evolution, Molecular ; Genes, Immunoglobulin ; Haptens/immunology ; Immunoglobulin Fab Fragments/genetics/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Immunoglobulin Light Chains/genetics/immunology ; Mice ; Molecular Sequence Data ; Mutation ; Protein Conformation
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  • 49
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    Discovering high-affinity ligands for proteins: SAR by NMR (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-29
    Description: A nuclear magnetic resonance (NMR)-based method is described in which small organic molecules that bind to proximal subsites of a protein are identified, optimized, and linked together to produce high-affinity ligands. The approach is called "SAR by NMR" because structure-activity relationships (SAR) are obtained from NMR. With this technique, compounds with nanomolar affinities for the FK506 binding protein were rapidly discovered by tethering two ligands with micromolar affinities. The method reduces the amount of chemical synthesis and time required for the discovery of high-affinity ligands and appears particularly useful in target-directed drug research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuker, S B -- Hajduk, P J -- Meadows, R P -- Fesik, S W -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1531-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929414" target="_blank"〉PubMed〈/a〉
    Keywords: Anilides/metabolism ; Binding Sites ; Carrier Proteins/*metabolism ; DNA-Binding Proteins/*metabolism ; Heat-Shock Proteins/*metabolism ; *Ligands ; *Magnetic Resonance Spectroscopy ; Models, Molecular ; Proteins/*metabolism ; Structure-Activity Relationship ; Tacrolimus/*metabolism ; Tacrolimus Binding Proteins
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  • 50
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    Structure of the A site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: Aminoglycoside antibiotics that bind to 30S ribosomal A-site RNA cause misreading of the genetic code and inhibit translocation. The aminoglycoside antibiotic paromomycin binds specifically to an RNA oligonucleotide that contains the 30S subunit A site, and the solution structure of the RNA-paromomycin complex was determined by nuclear magnetic resonance spectroscopy. The antibiotic binds in the major groove of the model A-site RNA within a pocket created by an A-A base pair and a single bulged adenine. Specific interactions occur between aminoglycoside chemical groups important for antibiotic activity and conserved nucleotides in the RNA. The structure explains binding of diverse aminoglycosides to the ribosome, their specific activity against prokaryotic organisms, and various resistance mechanisms, and provides insight into ribosome function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fourmy, D -- Recht, M I -- Blanchard, S C -- Puglisi, J D -- GM51266-01A1/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1367-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Center for Molecular Biology of RNA, University of California, Santa Cruz, CA 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910275" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/chemistry/*metabolism/pharmacology ; Base Composition ; Binding Sites ; Escherichia coli/drug effects/*genetics ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Methylation ; Models, Molecular ; *Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/metabolism ; Paromomycin/chemistry/*metabolism/pharmacology ; RNA, Bacterial/*chemistry/metabolism ; RNA, Ribosomal, 16S/*chemistry/metabolism ; Ribosomes/metabolism
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    DNA looping and lac repressor-CAP interaction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fried, M G -- Hudson, J M -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1930-1; author reply 1931-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984648" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/*metabolism ; Binding Sites ; Cyclic AMP Receptor Protein/chemistry/*metabolism ; DNA, Bacterial/chemistry/*metabolism ; Escherichia coli/genetics ; *Escherichia coli Proteins ; *Lac Operon ; Lac Repressors ; *Nucleic Acid Conformation ; Operator Regions, Genetic ; Protein Binding ; Protein Conformation ; Repressor Proteins/chemistry/*metabolism
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