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  • Protein Conformation  (54)
  • American Association for the Advancement of Science (AAAS)  (54)
  • Cell Press
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • 1990-1994  (54)
  • 1965-1969
  • 1991  (54)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (54)
  • Cell Press
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
Years
  • 1990-1994  (54)
  • 1965-1969
Year
  • 1
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    A phosphorylation site in the Na+ channel required for modulation by protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: Voltage-gated sodium channels are responsible for generation of action potentials in excitable cells. Activation of protein kinase C slows inactivation of sodium channels and reduces peak sodium currents. Phosphorylation of a single residue, serine 1506, that is located in the conserved intracellular loop between domains III and IV and is involved in inactivation of the sodium channel, is required for both modulatory effects. Mutant sodium channels lacking this phosphorylation site have normal functional properties in unstimulated cells but do not respond to activation of protein kinase C. Phosphorylation of this conserved site in sodium channel alpha subunits may regulate electrical activity in a wide range of excitable cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉West, J W -- Numann, R -- Murphy, B J -- Scheuer, T -- Catterall, W A -- GM07270/GM/NIGMS NIH HHS/ -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):866-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658937" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/physiology ; Cells, Cultured ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinase C/*metabolism ; Sodium Channels/metabolism/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-26
    Description: The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal structure of the complex is the basis of the analysis. The peptide inhibitor, derived from a naturally occurring heat-stable protein kinase inhibitor, contains an amphipathic helix that is followed by a turn and an extended conformation. The extended region occupies the cleft between the two lobes of the enzyme and contains a five-residue consensus recognition sequence common to all substrates and peptide inhibitors of the catalytic subunit. The helical portion of the peptide binds to a hydrophobic groove and conveys high affinity binding. Loops from both domains converge at the active site and contribute to a network of conserved residues at the sites of magnesium adenosine triphosphate binding and catalysis. Amino acids associated with peptide recognition, nonconserved, extend over a large surface area.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knighton, D R -- Zheng, J H -- Ten Eyck, L F -- Xuong, N H -- Taylor, S S -- Sowadski, J M -- RR01644/RR/NCRR NIH HHS/ -- T32CA09523/CA/NCI NIH HHS/ -- T32DK07233/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):414-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carrier Proteins/*chemistry/metabolism ; Computer Simulation ; Enzyme Inhibitors/*chemistry ; *Intracellular Signaling Peptides and Proteins ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Kinases/*chemistry/metabolism ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 3
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    Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 amino acids. It consists of a 12-stranded mixed beta sheet surrounded by 14 alpha helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sussman, J L -- Harel, M -- Frolow, F -- Oefner, C -- Goldman, A -- Toker, L -- Silman, I -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):872-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1678899" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/*metabolism ; Acetylcholinesterase/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/enzymology ; Chemistry, Physical ; Crystallization ; Electric Organ/*enzymology ; Glutamates ; Glutamic Acid ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Structure ; Phosphatidylinositols/metabolism ; Physicochemical Phenomena ; Protein Conformation ; Sequence Homology, Nucleic Acid ; *Torpedo ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-09
    Description: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milburn, M V -- Prive, G G -- Milligan, D L -- Scott, W G -- Yeh, J -- Jancarik, J -- Koshland, D E Jr -- Kim, S H -- AI 30725/AI/NIAID NIH HHS/ -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1342-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1660187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; Disulfides/analysis ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry/metabolism ; Salmonella typhimurium/metabolism ; X-Ray Diffraction
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  • 5
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    Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-22
    Description: Defensins (molecular weight 3500 to 4000) act in the mammalian immune response by permeabilizing the plasma membranes of a broad spectrum of target organisms, including bacteria, fungi, and enveloped viruses. The high-resolution crystal structure of defensin HNP-3 (1.9 angstrom resolution, R factor 0.19) reveals a dimeric beta sheet that has an architecture very different from other lytic peptides. The dimeric assembly suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, C P -- Yee, J -- Selsted, M E -- Eisenberg, D -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1481-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eisenberg, Molecular Biology Institute, Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006422" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blood Proteins/chemistry/*ultrastructure ; Cell Membrane Permeability ; Crystallography ; Defensins ; Guinea Pigs ; Humans ; Macromolecular Substances ; Membrane Proteins/chemistry/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Protein Conformation ; Rabbits ; Rats ; Structure-Activity Relationship ; X-Ray Diffraction ; *alpha-Defensins
    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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  • 6
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    Similarity of protein G and ubiquitin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kraulis, P J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):581-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658931" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites, Antibody ; Immunoglobulin G ; Models, Molecular ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/genetics/immunology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Ubiquitins/*chemistry/genetics
    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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  • 7
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    Specific DNA binding by c-Myb: evidence for a double helix-turn-helix-related motif (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-06
    Description: The c-Myb protein is a sequence-specific DNA binding protein that activates transcription in hematopoietic cells. Three imperfect repeats (R1, R2, and R3) that contain regularly spaced tryptophan residues form the DNA binding domain of c-Myb. A fragment of c-Myb that contained the R2 and R3 regions bound specifically to a DNA sequence recognized by c-Myb plus ten additional base pairs at the 3' end of the element. The R2R3 fragment was predicted to contain two consecutive helix-turn-helix (HTH) motifs with unconventional turns. Mutagenesis of amino acids in R2R3 at positions that correspond to DNA-contacting amino acids in other HTH-containing proteins abolished specific DNA binding without affecting nonspecific DNA interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabrielsen, O S -- Sentenac, A -- Fromageot, P -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Ingenierie des Proteines, Centre d'Etudes de Saclay, Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887237" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Chickens ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Oncogenes ; Polymerase Chain Reaction ; Protein Conformation ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-myb ; Recombinant Proteins/metabolism ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Transcription Factors/*metabolism
    Print ISSN: 0036-8075
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  • 8
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    Engineered metal-binding proteins: purification to protein folding (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnold, F H -- Haymore, B L -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1796-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648261" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carrier Proteins/*chemical synthesis/chemistry/isolation & purification ; Cytochrome c Group/chemistry ; Histidine ; Ligands ; Metals/*metabolism ; Models, Molecular ; Protein Conformation ; *Protein Engineering
    Print ISSN: 0036-8075
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  • 9
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    A component of calcium-activated potassium channels encoded by the Drosophila slo locus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-02
    Description: Calcium-activated potassium channels mediate many biologically important functions in electrically excitable cells. Despite recent progress in the molecular analysis of voltage-activated K+ channels, Ca(2+)-activated K+ channels have not been similarly characterized. The Drosophila slowpoke (slo) locus, mutations of which specifically abolish a Ca(2+)-activated K+ current in muscles and neurons, provides an opportunity for molecular characterization of these channels. Genomic and complementary DNA clones from the slo locus were isolated and sequenced. The polypeptide predicted by slo is similar to voltage-activated K+ channel polypeptides in discrete domains known to be essential for function. Thus, these results indicate that slo encodes a structural component of Ca(2+)-activated K+ channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Atkinson, N S -- Robertson, G A -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32 GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):551-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857984" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Chromosome Aberrations ; Chromosome Deletion ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Drosophila/*genetics/physiology ; Exons ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Phenotype ; Potassium Channels/drug effects/*genetics/physiology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Translocation, Genetic
    Print ISSN: 0036-8075
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  • 10
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    First protein kinase structure (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):383.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862341" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/chemistry/metabolism ; Enzyme Inhibitors/chemistry ; *Intracellular Signaling Peptides and Proteins ; Models, Molecular ; Protein Conformation ; Protein Kinases/*chemistry/metabolism
    Print ISSN: 0036-8075
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  • 11
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    Critical structural elements of the VP16 transcriptional activation domain (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-04
    Description: Virion protein 16 (VP16) of herpes simplex virus type 1 contains an acidic transcriptional activation domain. Missense mutations within this domain have provided insights into the structural elements critical for its function. Net negative charge contributed to, but was not sufficient for, transcriptional activation by VP16. A putative amphipathic alpha helix did not appear to be an important structural component of the activation domain. A phenylalanine residue at position 442 was exquisitely sensitive to mutation. Transcriptional activators of several classes contain hydrophobic amino acids arranged in patterns resembling that of VP16. Therefore, the mechanism of transcriptional activation by VP16 and other proteins may involve both ionic and specific hydrophobic interactions with target molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cress, W D -- Triezenberg, S J -- AI 27323/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):87-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Michigan State University, East Lansing 48824-1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846049" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Immediate-Early Proteins ; Molecular Sequence Data ; Mutation ; Protein Conformation ; *Simplexvirus ; Structure-Activity Relationship ; Transcription Factors/*chemistry/genetics/pharmacology ; Transcription, Genetic/*drug effects ; Transfection ; Viral Proteins/*genetics ; Virion
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  • 12
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    Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: Filamentous bacteriophage Pf1 assembles by a membrane-mediated process during which the viral DNA is secreted through the membrane while being encapsulated by the major coat protein. Neutron diffraction studies showed that in the virus most of the coat protein consists of two alpha-helical segments arranged end-to-end with an intervening mobile surface loop. Nuclear magnetic resonance studies of the coat protein in the membrane-bound form have shown that the secondary structure is essentially identical to that in the intact virus. A comparison indicates that during membrane-mediated viral assembly, while the secondary structure of the coat protein is largely conserved, its tertiary structure changes substantially.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nambudripad, R -- Stark, W -- Opella, S J -- Makowski, L -- New York, N.Y. -- Science. 1991 May 31;252(5010):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Boston University, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925543" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages/chemistry ; Capsid/*chemistry/metabolism ; *Capsid Proteins ; Cell Membrane/*metabolism ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Structure ; Neutrons ; Protein Conformation
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  • 13
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    Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-28
    Description: Human apolipoprotein E, a blood plasma protein, mediates the transport and uptake of cholesterol and lipid by way of its high affinity interaction with different cellular receptors, including the low-density lipoprotein (LDL) receptor. The three-dimensional structure of the LDL receptor-binding domain of apoE has been determined at 2.5 angstrom resolution by x-ray crystallography. The protein forms an unusually elongated (65 angstroms) four-helix bundle, with the helices apparently stabilized by a tightly packed hydrophobic core that includes leucine zipper-type interactions and by numerous salt bridges on the mostly charged surface. Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix. This structure provides the basis for understanding the behavior of naturally occurring mutants that can lead to atherosclerosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, C -- Wardell, M R -- Weisgraber, K H -- Mahley, R W -- Agard, D A -- HL-41633/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1817-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063194" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoproteins E/*chemistry/genetics/metabolism ; Binding Sites ; Computer Graphics ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Receptors, LDL/*metabolism ; X-Ray Diffraction
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  • 14
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    Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19. The tertiary structure of the subunit is similar to that of other legume lectins, but interference by the bulky N-linked heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure. Only the galactose moiety of the lactose ligand resides within the combining site. The galactose moiety is oriented differently from ligands in the mannose-glucose specific legume lectins and is held by hydrophobic interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107. The specificity of legume lectins toward the different C-4 epimers appears to be associated with extensive variations in the outline of the variable parts of the binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaanan, B -- Lis, H -- Sharon, N -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):862-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948067" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Conformation ; Carbohydrate Sequence ; Computer Simulation ; Erythrina ; Glycosylation ; Hydrogen Bonding ; Lectins/*chemistry ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides ; Plant Lectins ; Plants, Medicinal ; Protein Conformation ; X-Ray Diffraction
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  • 15
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    Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-31
    Description: The crystal structure of a murine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, has been determined and refined at 2.4 angstrom resolution. The structure is folded as an eight-stranded parallel alpha/beta barrel with a deep pocket at the beta-barrel COOH-terminal end wherein the inhibitor and a zinc are bound and completely sequestered. The presence of the zinc cofactor and the precise structure of the bound analog were not previously known. The 6R isomer of the analog is very tightly held in place by the coordination of the 6-hydroxyl to the zinc and the formation of nine hydrogen bonds. On the basis of the structure of the complex a stereoselective addition-elimination or SN2 mechanism of the enzyme is proposed with the zinc atom and the Glu and Asp residues playing key roles. A molecular explanation of a hereditary disease caused by several point mutations of an enzyme is also presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, D K -- Rudolph, F B -- Quiocho, F A -- CA14030/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1278-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925539" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/*chemistry/deficiency/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Catalysis ; Crystallization ; Immunologic Deficiency Syndromes/*enzymology/genetics ; Mice ; Models, Molecular ; Molecular Structure ; Mutation ; Protein Conformation ; Purine Nucleosides/chemistry/*metabolism ; Ribonucleosides/chemistry/*metabolism ; Zinc/metabolism
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  • 16
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    Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-06
    Description: Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K+ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel beta sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bontems, F -- Roumestand, C -- Gilquin, B -- Menez, A -- Toma, F -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1521-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement d'Ingenierie et d'Etudes des Proteines, Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blood Proteins/*ultrastructure ; Charybdotoxin ; Defensins ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Neurotoxins/*chemistry ; Potassium Channels/drug effects ; Protein Conformation ; Scorpion Venoms/*chemistry ; Scorpions ; Sequence Alignment
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  • 17
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    NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-31
    Description: Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles. Nuclear magnetic resonance (NMR) studies show the membrane-bound form of the 46-residue Pf1 coat protein to be surprisingly complex with five distinct regions. The secondary structure consists of a long hydrophobic helix (residues 19 to 42) that spans the bilayer and a short amphipathic helix (residues 6 to 13) parallel to the plane of the bilayer. The NH2-terminus (residues 1 to 5), the COOH-terminus (residues 43 to 46), and residues 14 to 18 connecting the two helices are mobile. By comparing the structure and dynamics of the membrane-bound coat protein with that of the viral form as determined by NMR and neutron diffraction, essential features of assembly process can be identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shon, K J -- Kim, Y -- Colnago, L A -- Opella, S J -- AI20770-06/AI/NIAID NIH HHS/ -- GM34343-06/GM/NIGMS NIH HHS/ -- RR-02301/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1303-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925542" target="_blank"〉PubMed〈/a〉
    Keywords: Capsid/*chemistry/metabolism ; *Capsid Proteins ; Cell Membrane/metabolism ; Lipid Bilayers/metabolism ; *Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Structure ; Protein Conformation
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  • 18
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    Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-22
    Description: The active site of voltage-activated potassium channels is a transmembrane aqueous pore that permits ions to permeate the cell membrane in a rapid yet highly selective manner. A useful probe for the pore of potassium-selective channels is the organic ion tetraethylammonium (TEA), which binds with millimolar affinity to the intracellular opening of the pore and blocks potassium current. In the potassium channel encoded by the Drosophila Shaker gene, an amino acid residue that specifically affects the affinity for intracellular TEA has now been identified by site-directed mutagenesis. This residue is in the middle of a conserved stretch of 18 amino acids that separates two locations that are both near the external opening of the pore. These findings suggest that this conserved region is intimately involved in the formation of the ion conduction pore of voltage-activated potassium channels. Further, a stretch of only eight amino acid residues must traverse 80 percent of the transmembrane electric potential difference.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yellen, G -- Jurman, M E -- Abramson, T -- MacKinnon, R -- GM4399/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):939-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000494" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Drosophila/genetics ; Genes ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; *Mutagenesis, Site-Directed ; Potassium Channels/drug effects/genetics/*physiology ; Protein Conformation ; Tetraethylammonium ; Tetraethylammonium Compounds/*pharmacology
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  • 19
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    Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-22
    Description: Three spatially distant surface loops were found to mediate the interaction of the coagulation protein factor X with the leukocyte integrin Mac-1. This interacting region, which by computational modeling defines a three-dimensional macromotif in the catalytic domain, was also recognized by glycoprotein C (gC), a factor X receptor expressed on herpes simplex virus (HSV)-infected endothelial cells. Peptidyl mimicry of each loop inhibited factor X binding to Mac-1 and gC, blocked monocyte generation of thrombin, and prevented monocyte adhesion to HSV-infected endothelium. These data link the ligand recognition of Mac-1 to established mechanisms of receptor-mediated vascular injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altieri, D C -- Etingin, O R -- Fair, D S -- Brunck, T K -- Geltosky, J E -- Hajjar, D P -- Edgington, T S -- HL 46408/HL/NHLBI NIH HHS/ -- P01 HL 16411/HL/NHLBI NIH HHS/ -- R01 HL 43773/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1200-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957171" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding, Competitive ; Cell Line ; Factor X/*metabolism/ultrastructure ; Humans ; In Vitro Techniques ; Ligands ; Macrophage-1 Antigen/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry/metabolism ; Protein Conformation ; Viral Envelope Proteins/*metabolism
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  • 20
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    Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-29
    Description: The three-dimensional structure of the activated state of glycogen phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP, although the two regulatory signals function through different local structural mechanisms. Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino- and carboxyl-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sprang, S R -- Withers, S G -- Goldsmith, E J -- Fletterick, R J -- Madsen, N B -- R01 DK26081/DK/NIDDK NIH HHS/ -- R01 DK31507/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1367-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962195" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/*pharmacology ; Amino Acid Sequence ; Binding Sites ; Enzyme Activation ; Macromolecular Substances ; Models, Molecular ; Phosphorylase b/chemistry/*metabolism ; Protein Conformation ; Pyridoxal Phosphate/analogs & derivatives/metabolism ; X-Ray Diffraction
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  • 21
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    1990: annus mirabilis of potassium channels (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-24
    Description: Voltage-gated potassium channels make up a large molecular family of integral membrane proteins that are fundamentally involved in the generation of bioelectric signals such as nerve impulses. These proteins span the cell membrane, forming potassium-selective pores that are rapidly switched open or closed by changes in membrane voltage. After the cloning of the first potassium channel over 3 years ago, recombinant DNA manipulation of potassium channel genes is now leading to a molecular understanding of potassium channel behavior. During the past year, functional domains responsible for channel gating and potassium selectivity have been identified, and detailed structural pictures underlying these functions are beginning to emerge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, C -- New York, N.Y. -- Science. 1991 May 24;252(5009):1092-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031183" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Amino Acid Sequence ; Animals ; Ion Channel Gating ; Models, Structural ; Molecular Sequence Data ; Potassium Channels/genetics/*physiology ; Protein Conformation
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  • 22
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    The energy landscapes and motions of proteins (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: Recent experiments, advances in theory, and analogies to other complex systems such as glasses and spin glasses yield insight into protein dynamics. The basis of the understanding is the observation that the energy landscape is complex: Proteins can assume a large number of nearly isoenergetic conformations (conformational substates). The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frauenfelder, H -- Sligar, S G -- Wolynes, P G -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1598-603.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Advanced Study, University of Illinois, Champaign, Urbana 61801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749933" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Monoxide/chemistry ; Chemistry, Physical ; Motion ; Myoglobin/*chemistry ; Physicochemical Phenomena ; Protein Conformation ; Structure-Activity Relationship ; Temperature ; Thermodynamics
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  • 23
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    Intrasubunit signal transduction by the aspartate chemoreceptor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-23
    Description: Receptors that transmit signals across cell membranes are typically composed of multiple subunits. To test whether subunit interactions are required for transmembrane signaling by the bacterial aspartate receptor, dimers were constructed with (i) two full-length subunits, (ii) one full-length subunit and one subunit lacking the cytoplasmic domain, or (iii) one full-length subunit and one subunit lacking both the cytoplasmic and the transmembrane domains. Methylation of the cytoplasmic domain of all three receptor constructs was stimulated by the binding of aspartate. These findings demonstrate that transmembrane signaling does not require interactions between cytoplasmic or transmembrane domains of adjacent subunits and suggest that signaling occurs via conformational changes transduced through a single subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milligan, D L -- Koshland, D E Jr -- DK 09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1651-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1661030" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/*physiology ; DNA Mutational Analysis ; Ligands ; Macromolecular Substances ; Methylation ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry ; Recombinant Proteins ; Salmonella typhimurium ; Signal Transduction ; Structure-Activity Relationship
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  • 24
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    New 3-D protein structures revealed. The shape of cholera (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, A -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):382-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862340" target="_blank"〉PubMed〈/a〉
    Keywords: Cholera Toxin/*chemistry ; Macromolecular Substances ; Models, Molecular ; Protein Conformation
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  • 25
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    Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-26
    Description: The 2.05 angstrom (A) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 A deep by 7 A wide) in an entropy-assisted association (association constant = 2.05 x 10(5) liters per mole, enthalpy = -20.5 +/- 1.7 kilojoules per mole, and temperature times entropy = +10.0 +/- 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine the antigen conformation adopted in the bound state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cygler, M -- Rose, D R -- Bundle, D R -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):442-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1713710" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Antigen-Antibody Complex ; Carbohydrate Conformation ; Carbohydrate Sequence ; Epitopes/chemistry ; Humans ; Immunoglobulin Fab Fragments/chemistry/*immunology ; Immunoglobulin G/classification/*immunology ; Lipopolysaccharides/chemistry/*immunology ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides/chemistry/*immunology ; Protein Conformation ; Salmonella/*immunology/pathogenicity
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  • 26
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    A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-09
    Description: The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gronenborn, A M -- Filpula, D R -- Essig, N Z -- Achari, A -- Whitlow, M -- Wingfield, P T -- Clore, G M -- New York, N.Y. -- Science. 1991 Aug 9;253(5020):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1871600" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/immunology ; Binding Sites ; Calorimetry ; Hydrogen Bonding ; *Immunoglobulin G ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; Protein Conformation
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  • 27
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    Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: Calcium-dependent (C-type) animal lectins participate in many cell surface recognition events mediated by protein-carbohydrate interactions. The C-type lectin family includes cell adhesion molecules, endocytic receptors, and extracellular matrix proteins. Mammalian mannose-binding proteins are C-type lectins that function in antibody-independent host defense against pathogens. The crystal structure of the carbohydrate-recognition domain of a rat mannose-binding protein, determined as the holmium-substituted complex by multiwavelength anomalous dispersion (MAD) phasing, reveals an unusual fold consisting of two distinct regions, one of which contains extensive nonregular secondary structure stabilized by two holmium ions. The structure explains the conservation of 32 residues in all C-type carbohydrate-recognition domains, suggesting that the fold seen here is common to these domains. The strong anomalous scattering observed at the Ho LIII edge demonstrates that traditional heavy atom complexes will be generally amenable to the MAD phasing method.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weis, W I -- Kahn, R -- Fourme, R -- Drickamer, K -- Hendrickson, W A -- GM34102/GM/NIGMS NIH HHS/ -- GM42628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1608-15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1721241" target="_blank"〉PubMed〈/a〉
    Keywords: Acute-Phase Proteins/*chemistry ; Amino Acid Sequence ; Animals ; Calcium/metabolism ; Calcium-Binding Proteins/*chemistry ; Carrier Proteins/*chemistry ; Collagen/chemistry ; Crystallography ; Holmium ; Hydrogen Bonding ; Lanthanum ; Lectins/*chemistry ; Ligands ; Mannose-Binding Lectins ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Protein Conformation ; Rats ; Recombinant Proteins/chemistry ; Sequence Alignment ; X-Ray Diffraction/methods
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    Molecular architecture and electrostatic properties of a bacterial porin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: The integral membrane protein porin from Rhodobacter capsulatus consists of three tightly associated 16-stranded beta barrels that give rise to three distinct diffusion channels for small solutes through the outer membrane. The x-ray structure of this porin has revealed details of its shape, the residue distributions within the pore and at the membrane-facing surface, and the location of calcium sites. The electrostatic potential has been calculated and related to function. Moreover, potential calculations were found to predict the Ca2+ sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, M S -- Abele, U -- Weckesser, J -- Welte, W -- Schiltz, E -- Schulz, G E -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1627-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Organische Chemie und Biochemie, Freiburg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1721242" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*chemistry ; Calcium/metabolism ; Calcium-Binding Proteins/metabolism ; Computer Graphics ; Crystallography ; Ion Channels/*chemistry ; Ions ; Macromolecular Substances ; Models, Molecular ; Molecular Structure ; Porins ; Protein Conformation ; Rhodobacter capsulatus/*chemistry ; X-Ray Diffraction
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    Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-20
    Description: Granulocyte-macrophage colony-stimulating factor (GM-CSF) stimulates the development of and the cytotoxic activity of white blood cells. Recombinant human GM-CSF has proven useful in the treatment of blood disorders. The structure of GM-CSF, which was determined at 2.4 angstrom resolution by x-ray crystallography, has a novel fold combining a two-stranded antiparallel beta sheet with an open bundle of four alpha helices. Residues implicated in receptor recognition, which are distant in the primary sequence, are on adjacent alpha helices in the folded protein. A working model for the receptor binding site is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diederichs, K -- Boone, T -- Karplus, P A -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1779-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1837174" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Granulocyte-Macrophage Colony-Stimulating Factor/*chemistry/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Receptors, Granulocyte-Macrophage Colony-Stimulating Factor/*chemistry/metabolism ; X-Ray Diffraction
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    X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, E K -- Klemm, J D -- Kim, P S -- Alber, T -- GM 44162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):539-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948029" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Computer Simulation ; DNA-Binding Proteins/*chemistry ; Fungal Proteins/*chemistry ; Hydrogen Bonding ; *Leucine Zippers ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Protein Kinases ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*chemistry ; X-Ray Diffraction
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    Three-dimensional structure of recombinant human interferon-gamma (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-03
    Description: The x-ray crystal structure of recombinant human interferon-gamma has been determined with the use of multiple-isomorphous-replacement techniques. Interferon-gamma, which is dimeric in solution, crystallizes with two dimers related by a noncrystallographic twofold axis in the asymmetric unit. The protein is primarily alpha helical, with six helices in each subunit that comprise approximately 62 percent of the structure; there is no beta sheet. The dimeric structure of human interferon-gamma is stabilized by the intertwining of helices across the subunit interface with multiple intersubunit interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ealick, S E -- Cook, W J -- Vijay-Kumar, S -- Carson, M -- Nagabhushan, T L -- Trotta, P P -- Bugg, C E -- CA-13148/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):698-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902591" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallization ; Glycosylation ; Humans ; Interferon-gamma/*chemistry ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Recombinant Proteins ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction
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    Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-04
    Description: The three-dimensional structure of spinach ferredoxin-NADP+ reductase (NADP+, nicotinamide adenine dinucleotide phosphate) has been determined by x-ray diffraction at 2.6 angstroms (A) resolution and initially refined to an R factor of 0.226 at 2.2 A resolution. The model includes the flavin-adenine dinucleotide (FAD) prosthetic group and the protein chain from residue 19 through the carboxyl terminus at residue 314 and is composed of two domains. The FAD binding domain (residues 19 to 161) has an antiparallel beta barrel core and a single alpha helix for binding the pyrophosphate of FAD. The NADP binding domain (residues 162 to 314) has a central five-strand parallel beta sheet and six surrounding helices. Binding of the competitive inhibitor 2'-phospho-AMP (AMP, adenosine monophosphate) places the NADP binding site at the carboxyl-terminal edge of the sheet in a manner similar to the nucleotide binding of the dehydrogenase family. The structures reveal the key residues that function in cofactor binding and the catalytic center. With these key residues as a guide, conclusive evidence is presented that the ferredoxin reductase structure is a prototype for the nicotinamide dinucleotide and FAD binding domains of the enzymes NADPH-cytochrome P450 reductase, NADPH-sulfite reductase, NADH-cytochrome b5 reductase, and NADH-nitrate reductase. Thus this structure provides a structural framework for the NADH- or NADPH-dependent flavoenzyme parts of five distinct enzymes involved in photosynthesis, in the assimilation of inorganic nitrogen and sulfur, in fatty-acid oxidation, in the reduction of methemoglobin, and in the metabolism of many pesticides, drugs, and carcinogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karplus, P A -- Daniels, M J -- Herriott, J R -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):60-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1986412" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Crystallization ; Ferredoxin-NADP Reductase/*chemistry ; Ferredoxins/metabolism ; Flavin-Adenine Dinucleotide/metabolism ; Hydrogen Bonding ; Molecular Sequence Data ; Molecular Structure ; NADP/metabolism ; Nucleotides/metabolism ; Plants/enzymology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction
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    Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: The 3 angstrom resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with a 30-base pair DNA sequence shows that the DNA is bent by 90 degrees. This bend results almost entirely from two 40 degrees kinks that occur between TG/CA base pairs at positions 5 and 6 on each side of the dyad axis of the complex. DNA sequence discrimination by CAP derives both from sequence-dependent distortion of the DNA helix and from direct hydrogen-bonding interactions between three protein side chains and the exposed edges of three base pairs in the major groove of the DNA. The structure of this transcription factor--DNA complex provides insights into possible mechanisms of transcription activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, S C -- Shields, G C -- Steitz, T A -- GM-22778/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1001-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1653449" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Cyclic AMP Receptor Protein/*chemistry/metabolism ; DNA, Bacterial/*chemistry/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; X-Ray Diffraction/methods
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    Protein electron transfer rates set by the bridging secondary and tertiary structure (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-31
    Description: The rate of long-distance electron transfer in proteins rapidly decreases with distance, which is indicative of an electron tunneling process. Calculations predict that the distance dependence of electron transfer in native proteins is controlled by the protein's structural motif. The helix and sheet content of a protein and the tertiary arrangement of these secondary structural units define the distance dependence of electronic coupling in that protein. The calculations use a tunneling pathway model applied previously with success to ruthenated proteins. The analysis ranks the average distance decay constant for electronic coupling in electron transfer proteins and identifies the amino acids that are coupled to the charge localization site more strongly or weakly than average for their distance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beratan, D N -- Betts, J N -- Onuchic, J N -- New York, N.Y. -- Science. 1991 May 31;252(5010):1285-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beratan, Jet Propulsion Laboratory, California Institute of Technology, Pasadena 91109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656523" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/chemistry ; Azurin/chemistry/metabolism ; *Bacterial Proteins ; Chemistry, Physical ; Cytochrome c Group/chemistry/metabolism ; Cytochromes b5/chemistry/metabolism ; *Electron Transport ; Iron-Sulfur Proteins/chemistry/metabolism ; Mathematics ; Models, Molecular ; Myoglobin/chemistry/metabolism ; *Photosynthetic Reaction Center Complex Proteins ; Physicochemical Phenomena ; Protein Conformation ; Proteins/*chemistry/metabolism ; Structure-Activity Relationship
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    Three-dimensional structures of acidic and basic fibroblast growth factors (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-04
    Description: Members of the fibroblast growth factor (FGF) family of proteins stimulate the proliferation and differentiation of a variety of cell types through receptor-mediated pathways. The three-dimensional structures of two members of this family, bovine acidic FGF and human basic FGF, have been crystallographically determined. These structures contain 12 antiparallel beta strands organized into a folding pattern with approximate threefold internal symmetry. Topologically equivalent folds have been previously observed for soybean trypsin inhibitor and interleukins-1 beta and -1 alpha. The locations of sequences implicated in receptor and heparin binding by FGF are presented. These sites include beta-sheet strand 10, which is adjacent to the site of an extended sequence insertion in several oncogene proteins of the FGF family, and which shows sequence conservation among the FGF family and interleukin-1 beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, X -- Komiya, H -- Chirino, A -- Faham, S -- Fox, G M -- Arakawa, T -- Hsu, B T -- Rees, D C -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):90-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1702556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Chemistry, Physical ; Crystallization ; Fibroblast Growth Factor 1/*chemistry/metabolism ; Fibroblast Growth Factor 2/*chemistry/metabolism ; Heparin/metabolism ; Humans ; Interleukin-1/chemistry ; Molecular Sequence Data ; Molecular Structure ; Physicochemical Phenomena ; Protein Conformation ; Recombinant Proteins/chemistry ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction
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    A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-25
    Description: An in vitro assay for the interaction of SecB, a molecular chaperone from Escherichia coli, with polypeptide ligands was established based on the ability of SecB to block the refolding of denatured maltose-binding protein. Competition experiments show that SecB binds selectively to nonnative proteins with high affinity and without specificity for a particular sequence of amino acids. It is proposed that selectivity in binding is due to a kinetic partitioning of polypeptides between folding and association with SecB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardy, S J -- Randall, L L -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):439-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1989077" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Bacterial Proteins/*metabolism ; Binding, Competitive ; Carrier Proteins/*metabolism ; *Escherichia coli ; *Escherichia coli Proteins ; Kinetics ; Ligands ; Maltose/metabolism ; Maltose-Binding Proteins ; *Monosaccharide Transport Proteins ; Protein Conformation
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    Dimerization of human growth hormone by zinc (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-02
    Description: Size-exclusion chromatography and sedimentation equilbrium studies demonstrated that zinc ion (Zn2+) induced the dimerization of human growth hormone (hGH). Scatchard analysis of 65Zn2+ binding to hGH showed that two Zn2+ ions associate per dimer of hGH in a cooperative fashion. Cobalt (II) can substitute for Zn2+ in the hormone dimer and gives a visible spectrum characteristic of cobalt coordinated in a tetrahedral fashion by oxygen- and nitrogen-containing ligands. Replacement of potential Zn2+ ligands (His18, His21, and Glu174) in hGH with alanine weakened both Zn2+ binding and hGH dimer formation. The Zn(2+)-hGH dimer was more stable than monomeric hGH to denaturation in guanidine-HCl. Formation of a Zn(2+)-hGH dimeric complex may be important for storage of hGH in secretory granules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B C -- Mulkerrin, M G -- Wells, J A -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):545-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1907025" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Chromatography, Gel ; Edetic Acid/pharmacology ; Growth Hormone/*metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Denaturation ; Spectrophotometry ; Zinc/metabolism/*pharmacology
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    Dimers direct development (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1176-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848724" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/*metabolism ; Drosophila ; Mammals ; Models, Structural ; Muscle Proteins/genetics ; MyoD Protein ; Protein Conformation
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  • 39
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    Identification and characterization of zinc binding sites in protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-20
    Description: Metal ion coordination in the regulatory domain of protein kinase C (PKC) is suggested by the conservation of six cysteines and two histidines in two homologous regions found therein. By monitoring x-ray fluorescence from a purified sample of rat PKC beta I overexpressed in insect cells, direct evidence has been obtained that PKC beta I tightly binds four zinc ions (Zn2+) per molecule. Extended x-ray absorption fine structure (EXAFS) data are best fit by an average Zn2+ coordination of one nitrogen and three sulfur atoms. Of the plausible Zn2+ coordination models, only those featuring nonbridged Zn2+ sites accommodate the EXAFS data and all of the conserved potential ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hubbard, S R -- Bishop, W R -- Kirschmeier, P -- George, S J -- Cramer, S P -- Hendrickson, W A -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1776-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, New York, NY.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763327" target="_blank"〉PubMed〈/a〉
    Keywords: Absorptiometry, Photon/methods ; Amino Acid Sequence ; Animals ; Binding Sites ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Protein Conformation ; Protein Kinase C/chemistry/genetics/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology, Nucleic Acid ; Zinc/*metabolism
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    Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-04-05
    Description: The crystal structure of the ribonuclease (RNase) H domain of HIV-1 reverse transcriptase (RT) has been determined at a resolution of 2.4 A and refined to a crystallographic R factor of 0.20. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The overall structure is similar in most respects to the RNase H from Escherichia coli. Structural features characteristic of the retroviral protein suggest how it may interface with the DNA polymerase domain of p66 in the mature RT heterodimer. These features also offer insights into why the isolated RNase H domain is catalytically inactive but when combined in vitro with the isolated p51 domain of RT RNase H activity can be reconstituted. Surprisingly, the peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of p66 is completely inaccessible to solvent in the structure reported here. This suggests that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davies, J F 2nd -- Hostomska, Z -- Hostomsky, Z -- Jordan, S R -- Matthews, D A -- GM 39599/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 5;252(5002):88-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Agouron Pharmaceuticals, Inc., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1707186" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Computer Graphics ; Crystallography ; Endoribonucleases/chemistry/*ultrastructure ; Escherichia coli/enzymology ; HIV-1/*enzymology ; Manganese/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; RNA-Directed DNA Polymerase/chemistry/*ultrastructure ; Ribonuclease H ; Structure-Activity Relationship ; X-Ray Diffraction
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    Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: The secondary structures in solution of the synthetic, naturally occurring, amyloid beta peptides, residues 1 to 42 [beta (1-42)] and beta (1-39), and related fragments, beta (1-28) and beta (29-42), have been studied by circular dichroism and two-dimensional nuclear magnetic resonance spectroscopy. In patients with Alzheimer's disease, extracellular amyloid plaque core is primarily composed of beta (1-42), whereas cerebrovascular amyloid contains the more soluble beta (1-39). In aqueous trifluoroethanol solution, the beta (1-28), beta (1-39), and beta (1-42) peptides adopt monomeric alpha-helical structures at both low and high pH, whereas at intermediate pH (4 to 7) an oligomeric beta structure (the probable structure in plaques) predominates. Thus, beta peptide is not by itself an insoluble protein (as originally thought), and localized or normal age-related alterations of pH may be necessary for the self-assembly and deposition of beta peptide. The hydrophobic carboxyl-terminal segment, beta(29-42), exists exclusively as an oligomeric beta sheet in solution, regardless of differences in solvent, pH, or temperature, suggesting that this segment directs the folding of the complete beta (1-42) peptide to produce the beta-pleated sheet found in amyloid plaques.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrow, C J -- Zagorski, M G -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):179-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Suntory Institute for Bioorganic Research, Osaka, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853202" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*pathology ; Amino Acid Sequence ; Amyloid beta-Peptides/*chemistry ; Circular Dichroism ; Humans ; In Vitro Techniques ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Peptides/chemistry ; Protein Conformation
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  • 42
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    A distinct potassium channel polypeptide encoded by the Drosophila eag locus (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-14
    Description: Many of the signaling properties of neurons and other electrically excitable cells are determined by a diverse family of potassium channels. A number of genes that encode potassium channel polypeptides have been cloned from various organisms on the basis of their sequence similarity to the Drosophila Shaker (Sh) locus. As an alternative strategy, a molecular analysis of other Drosophila genes that were defined by mutations that perturb potassium channel function was undertaken. Sequence analysis of complementary DNA from the ether a go-go (eag) locus revealed that it encodes a structural component of potassium channels that is related to but is distinct from all identified potassium channel polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warmke, J -- Drysdale, R -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1560-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840699" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; DNA/genetics ; Drosophila/*genetics ; Molecular Sequence Data ; Potassium Channels/*genetics ; Protein Conformation ; Sequence Homology, Nucleic Acid
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  • 43
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    Reexamination of the folding of BPTI: predominance of native intermediates (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-09-20
    Description: Bovine pancreatic trypsin inhibitor (BPTI) continues to be the only protein for which a detailed pathway of folding has been described. Previous studies led to the conclusion that nonnative states are well populated in the oxidative folding of BPTI. This conclusion has broadly influenced efforts to understand protein folding. The population of intermediates present during the folding of BPTI has been reexamined by modern separation techniques. It was found that all well-populated folding intermediates contain only native disulfide bonds. These data emphasize the importance of native protein structure for understanding protein folding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weissman, J S -- Kim, P S -- GM 41307/GM/NIGMS NIH HHS/ -- RR 05927/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1386-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716783" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aprotinin/*chemistry ; Chromatography, High Pressure Liquid ; Disulfides/analysis ; Indicators and Reagents ; Models, Structural ; Molecular Sequence Data ; Peptide Fragments/isolation & purification ; Protein Conformation
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  • 44
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    Cloning and expression of a cocaine-sensitive dopamine transporter complementary DNA (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: A rat dopamine (DA) transporter complementary DNA has been isolated with combined complementary DNA homology and expression approaches. The DA transporter is a 619-amino acid protein with 12 hydrophobic putative membrane-spanning domains and homology to the norepinephrine and gamma-aminobutyric acid transporters. The expressed complementary DNA confers transport of [3H]DA in Xenopus oocytes and in COS cells. Binding of the cocaine analog [3H]CFT ([3H]2 beta-carbomethoxy-3 beta-(4-fluorophenyl)tropane) to transfected COS cell membranes yields a pharmacological profile similar to that in striatal membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimada, S -- Kitayama, S -- Lin, C L -- Patel, A -- Nanthakumar, E -- Gregor, P -- Kuhar, M -- Uhl, G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):576-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology, National Institute on Drug Abuse, Baltimore, MD 21224.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948034" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cloning, Molecular ; Cocaine/analogs & derivatives/metabolism/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Female ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Models, Structural ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Oocytes/physiology ; Plasmids ; Polymerase Chain Reaction ; Protein Conformation ; RNA, Messenger/genetics ; Rats ; Transcription, Genetic ; Transfection ; Xenopus
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  • 45
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    Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-29
    Description: Molecular self-assembly is the spontaneous association of molecules under equilibrium conditions into stable, structurally well-defined aggregates joined by noncovalent bonds. Molecular self-assembly is ubiquitous in biological systems and underlies the formation of a wide variety of complex biological structures. Understanding self-assembly and the associated noncovalent interactions that connect complementary interacting molecular surfaces in biological aggregates is a central concern in structural biochemistry. Self-assembly is also emerging as a new strategy in chemical synthesis, with the potential of generating nonbiological structures with dimensions of 1 to 10(2) nanometers (with molecular weights of 10(4) to 10(10) daltons). Structures in the upper part of this range of sizes are presently inaccessible through chemical synthesis, and the ability to prepare them would open a route to structures comparable in size (and perhaps complementary in function) to those that can be prepared by microlithography and other techniques of microfabrication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitesides, G M -- Mathias, J P -- Seto, C T -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1312-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962191" target="_blank"〉PubMed〈/a〉
    Keywords: Biotechnology/methods ; DNA/chemical synthesis/*chemistry ; Models, Chemical ; Models, Molecular ; Protein Conformation ; Proteins/chemical synthesis/*chemistry ; Thermodynamics ; Triazines/chemical synthesis/chemistry
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  • 46
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    Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-15
    Description: Phospholipase A2 (PLA2) participates in a wide range of cellular processes including inflammation and transmembrane signaling. A human nonpancreatic secretory PLA2 (hnps-PLA2) has been identified that is found in high concentrations in the synovial fluid of patients with rheumatoid arthritis and in the plasma of patients with septic shock. This enzyme is secreted from certain cell types in response to the proinflammatory cytokines, tumor necrosis factor or interleukin-1. The crystal structures of the calcium-bound form of this enzyme have been determined at physiological pH both in the presence [2.1 angstrom (A) resolution] and absence (2.2 A resolution) of a transition-state analogue. Although the critical features that suggest the chemistry of catalysis are identical to those inferred from the crystal structures of other extracellular PLA2s, the shape of the hydrophobic channel of hnps-PLA2 is uniquely modulated by substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, D L -- White, S P -- Browning, J L -- Rosa, J J -- Gelb, M H -- Sigler, P B -- GM22324/GM/NIGMS NIH HHS/ -- HL36235/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1007-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948070" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/chemistry ; Computer Graphics ; Crystallography ; Extracellular Space/enzymology ; Humans ; Inflammation/*enzymology ; Molecular Sequence Data ; Phospholipases A/antagonists & inhibitors/*ultrastructure ; Phospholipases A2 ; Protein Conformation ; Recombinant Proteins ; Sequence Alignment ; X-Ray Diffraction
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  • 47
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    Finding a new target for AIDS therapy (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1991 Apr 5;252(5002):31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1849317" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/therapy ; Crystallography ; Endoribonucleases/*ultrastructure ; HIV-1/*enzymology ; Humans ; Protein Conformation ; Ribonuclease H
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  • 48
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    Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-26
    Description: The structure of kistrin, which is a member of a homologous family of glycoprotein IIb-IIIa (GP IIb-IIIa) antagonists and potent protein inhibitors of platelet aggregation, has been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The 68-residue protein consists of a series of tightly packed loops held together by six disulfide bonds and has almost no regular secondary structure. Kistrin has an Arg-Gly-Asp (RGD) adhesion site recognition sequence important for binding to GP IIb-IIIa that is located at the apex of a long loop across the surface of the protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adler, M -- Lazarus, R A -- Dennis, M S -- Wagner, G -- GM38608/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):445-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862345" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Glycoproteins/*chemistry ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptides/*chemistry/genetics ; Platelet Aggregation Inhibitors/*chemistry ; Platelet Membrane Glycoproteins/*antagonists & inhibitors ; Protein Conformation
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  • 49
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    Identification of FAP locus genes from chromosome 5q21 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-09
    Description: Recent studies suggest that one or more genes on chromosome 5q21 are important for the development of colorectal cancers, particularly those associated with familial adenomatous polyposis (FAP). To facilitate the identification of genes from this locus, a portion of the region that is tightly linked to FAP was cloned. Six contiguous stretches of sequence (contigs) containing approximately 5.5 Mb of DNA were isolated. Subclones from these contigs were used to identify and position six genes, all of which were expressed in normal colonic mucosa. Two of these genes (APC and MCC) are likely to contribute to colorectal tumorigenesis. The MCC gene had previously been identified by virtue of its mutation in human colorectal tumors. The APC gene was identified in a contig initiated from the MCC gene and was found to encode an unusually large protein. These two closely spaced genes encode proteins predicted to contain coiled-coil regions. Both genes were also expressed in a wide variety of tissues. Further studies of MCC and APC and their potential interaction should prove useful for understanding colorectal neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kinzler, K W -- Nilbert, M C -- Su, L K -- Vogelstein, B -- Bryan, T M -- Levy, D B -- Smith, K J -- Preisinger, A C -- Hedge, P -- McKechnie, D -- CA06973/CA/NCI NIH HHS/ -- CA35494/CA/NCI NIH HHS/ -- CA44688/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 9;253(5020):661-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Genetics Laboratory, Johns Hopkins University School of Medicine, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1651562" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/*genetics ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 5 ; Colon/physiology ; Colonic Neoplasms/genetics ; Exons ; Gene Expression ; Humans ; Intestinal Mucosa/*physiology ; Molecular Sequence Data ; Muscles/physiology ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Probability ; Protein Conformation ; Receptors, Cholinergic/physiology ; Restriction Mapping ; Sequence Homology, Nucleic Acid
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    Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120 (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-04
    Description: The spectrum of human immunodeficiency virus type 1 (HIV-1) isolates neutralized by antibodies from HIV-1-infected humans is broader than the spectrum of isolates neutralized by sera from animals immunized with purified gp120 subunits. This broader neutralization was due, in part, to the presence of antibodies to conserved gp120 conformational epitopes. Purified conformation-dependent gp120-specific human antibodies neutralized a wider range of virus isolates than human antibodies directed to linear determinants in gp120 and were also responsible for the majority of the gp120-specific CD4-blocking activity of HIV-1-infected human sera. A gp120 subunit vaccine that effectively presents these conformation-dependent neutralization epitopes should protect against a broader range of HIV-1 variants than a vaccine that presents exclusively linear determinants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steimer, K S -- Scandella, C J -- Skiles, P V -- Haigwood, N L -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):105-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chiron Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibody Specificity ; Epitopes ; Gene Products, env/immunology ; HIV Antibodies/chemistry/*immunology ; HIV Envelope Protein gp120/chemistry/*immunology ; HIV-1/*immunology ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Neutralization Tests ; Protein Conformation ; Structure-Activity Relationship
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    Methylation-sensitive sequence-specific DNA binding by the c-Myc basic region (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-11
    Description: The function of the c-Myc oncoprotein and its role in cell growth control is unclear. A basic region of c-Myc is structurally related to the basic motifs of helix-loop-helix (HLH) and leucine zipper proteins, which provide sequence-specific DNA binding function. The c-Myc basic region was tested for its ability to bind DNA by attaching it to the HLH dimerization interface of the E12 enhancer binding factor. Dimers of the chimeric protein, termed E6, specifically bound an E box element (GGCCACGTGACC) recognized by other HLH proteins in a manner dependent on the integrity of the c-Myc basic motif. Methylation of the core CpG in the E box recognition site specifically inhibited binding by E6, but not by two other HLH proteins. Expression of E6 (but not an E6 DNA binding mutant) suppressed the ability of c-myc to cooperate with H-ras in a rat embryo fibroblast transformation assay, suggesting that the DNA recognition specificity of E6 is related to that of c-Myc in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prendergast, G C -- Ziff, E B -- New York, N.Y. -- Science. 1991 Jan 11;251(4990):186-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, New York, NY.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987636" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA/*metabolism ; DNA-Binding Proteins/genetics/metabolism ; Genes, ras ; Leucine Zippers ; Macromolecular Substances ; Methylation ; Molecular Sequence Data ; Mutagenesis ; Oligonucleotide Probes ; Protein Conformation ; Proto-Oncogene Proteins c-myc/genetics/*metabolism ; Rabbits ; Rats ; Recombinant Fusion Proteins/metabolism
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  • 52
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    Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp) (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: The crystal structure of the binary complex tRNA(Asp)-aspartyl tRNA synthetase from yeast was solved with the use of multiple isomorphous replacement to 3 angstrom resolution. The dimeric synthetase, a member of class II aminoacyl tRNA synthetases (aaRS's) exhibits the characteristic signature motifs conserved in eight aaRS's. These three sequence motifs are contained in the catalytic site domain, built around an antiparallel beta sheet, and flanked by three alpha helices that form the pocket in which adenosine triphosphate (ATP) and the CCA end of tRNA bind. The tRNA(Asp) molecule approaches the synthetase from the variable loop side. The two major contact areas are with the acceptor end and the anticodon stem and loop. In both sites the protein interacts with the tRNA from the major groove side. The correlation between aaRS class II and the initial site of aminoacylation at 3'-OH can be explained by the structure. The molecular association leads to the following features: (i) the backbone of the GCCA single-stranded portion of the acceptor end exhibits a regular helical conformation; (ii) the loop between residues 320 and 342 in motif 2 interacts with the acceptor stem in the major groove and is in contact with the discriminator base G and the first base pair UA; and (iii) the anticodon loop undergoes a large conformational change in order to bind the protein. The conformation of the tRNA molecule in the complex is dictated more by the interaction with the protein than by its own sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruff, M -- Krishnaswamy, S -- Boeglin, M -- Poterszman, A -- Mitschler, A -- Podjarny, A -- Rees, B -- Thierry, J C -- Moras, D -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1682-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Cristallographie Biologique, Institut de Biologie Moleculaire et Cellulaire du CNRS, Universite Louis Pasteur, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047877" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartate-tRNA Ligase/classification/*ultrastructure ; Base Sequence ; Binding Sites ; Computer Graphics ; Crystallography ; Fungal Proteins/*ultrastructure ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; RNA, Fungal/ultrastructure ; RNA, Transfer, Amino Acyl/metabolism/ultrastructure ; RNA, Transfer, Asp/metabolism/*ultrastructure ; Saccharomyces cerevisiae/enzymology ; X-Ray Diffraction
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    The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-26
    Description: The three-dimensional crystal structure of the copper-containing nitrite reductase (NIR) from Achromobacter cycloclastes has been determined to 2.3 angstrom (A) resolution by isomorphous replacement. The monomer has two Greek key beta-barrel domains similar to that of plastocyanin and contains two copper sites. The enzyme is a trimer both in the crystal and in solution. The two copper atoms in the monomer comprise one type I copper site (Cu-I; two His, one Cys, and one Met ligands) and one putative type II copper site (Cu-II; three His and one solvent ligands). Although ligated by adjacent amino acids Cu-I and Cu-II are approximately 12.5 A apart. Cu-II is bound with nearly perfect tetrahedral geometry by residues not within a single monomer, but from each of two monomers of the trimer. The Cu-II site is at the bottom of a 12 A deep solvent channel and is the site to which the substrate (NO2-) binds, as evidenced by difference density maps of substrate-soaked and native crystals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Godden, J W -- Turley, S -- Teller, D C -- Adman, E T -- Liu, M Y -- Payne, W J -- LeGall, J -- GM08268-02/GM/NIGMS NIH HHS/ -- GM31770/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):438-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862344" target="_blank"〉PubMed〈/a〉
    Keywords: Alcaligenes/*enzymology ; Amino Acid Sequence ; Copper/analysis ; Models, Molecular ; Molecular Weight ; Nitrite Reductases/*chemistry ; Protein Conformation ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 54
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    Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: Human growth hormone (hGH) forms a 1:2 complex with the extracellular domain of its receptor-binding protein (hGHbp) as studied by crystallization, size exclusion chromatography, calorimetry, and a previously undescribed fluorescence quenching assay. These and other experiments with protein engineered variants of hGH have led to the identification of the binding determinants for two distinct but adjacent sites on hGH for the hGHbp, and the data indicated that there are two overlapping binding sites on the hGHbp for hGH. Furthermore, the binding of hGH to the hGHbp occurred sequentially; a first hGHbp molecule bound to site 1 on hGH and then a second hGHbp bound to site 2. Hormone-induced receptor dimerization is proposed to be relevant to the signal transduction mechanism for the hGH receptor and other related cytokine receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B C -- Ultsch, M -- De Vos, A M -- Mulkerrin, M G -- Clauser, K R -- Wells, J A -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):821-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948064" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Binding Sites ; Chromatography, Gel ; Growth Hormone/*metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Models, Structural ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Receptors, Somatotropin/genetics/isolation & purification/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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