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  • Models, Molecular
  • American Association for the Advancement of Science (AAAS)  (14)
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • Nature Publishing Group (NPG)
  • 2005-2009
  • 1985-1989  (14)
  • 1987  (14)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (14)
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • Nature Publishing Group (NPG)
Years
  • 2005-2009
  • 1985-1989  (14)
Year
  • 1
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    Generation of a hybrid sequence-specific single-stranded deoxyribonuclease (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-04
    Description: The relatively nonspecific single-stranded deoxyribonuclease, staphylococcal nuclease, was selectively fused to an oligonucleotide binding site of defined sequence to generate a hybrid enzyme. A cysteine was substituted for Lys116 in the enzyme by oligonucleotide-directed mutagenesis and coupled to an oligonucleotide that contained a 3'-thiol. The resulting hybrid enzyme cleaved single-stranded DNA at sites adjacent to the oligonucleotide binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D R -- Schultz, P G -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1401-3.〈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/3685986" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Single-Stranded/metabolism ; Hydrolysis ; Micrococcal Nuclease/*genetics/metabolism ; Models, Molecular ; Mutation ; Protein Conformation ; Staphylococcus aureus/enzymology/genetics ; Substrate Specificity
    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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    Chemistry in the image of biology (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):611-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672114" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; *Chemistry ; Models, Molecular ; *Nobel Prize
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  • 3
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    Structure of MHC protein solved (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):613-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3313727" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens ; Binding Sites ; *HLA Antigens ; Humans ; Models, Molecular ; Protein Conformation
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  • 4
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    Synthesis of a sequence-specific DNA-cleaving peptide (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-20
    Description: A synthetic 52-residue peptide based on the sequence-specific DNA-binding domain of Hin recombinase (139-190) has been equipped with ethylenediaminetetraacetic acid (EDTA) at the amino terminus. In the presence of Fe(II), this synthetic EDTA-peptide cleaves DNA at Hin recombination sites. The cleavage data reveal that the amino terminus of Hin(139-190) is bound in the minor groove of DNA near the symmetry axis of Hin recombination sites. This work demonstrates the construction of a hybrid peptide combining two functional domains: sequence-specific DNA binding and DNA cleavage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sluka, J P -- Horvath, S J -- Bruist, M F -- Simon, M I -- Dervan, P B -- GM-09534-02/GM/NIGMS NIH HHS/ -- T32GM07616/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1129-32.〈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/3120311" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; DNA/*metabolism ; DNA Nucleotidyltransferases/*metabolism ; DNA-Binding Proteins/*chemical synthesis ; Edetic Acid ; Ferrous Compounds ; Models, Molecular ; Nucleic Acid Conformation ; Oxidation-Reduction ; Peptide Fragments ; Protein Binding ; Structure-Activity Relationship
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  • 5
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    Identification of a family of muscarinic acetylcholine receptor genes (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-31
    Description: Complementary DNAs for three different muscarinic acetylcholine receptors were isolated from a rat cerebral cortex library, and the cloned receptors were expressed in mammalian cells. Analysis of human and rat genomic clones indicates that there are at least four functional muscarinic receptor genes and that these genes lack introns in the coding sequence. This gene family provides a new basis for evaluating the diversity of muscarinic mechanisms in the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonner, T I -- Buckley, N J -- Young, A C -- Brann, M R -- New York, N.Y. -- Science. 1987 Jul 31;237(4814):527-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/metabolism ; Cloning, Molecular ; Codon ; Dna ; DNA Restriction Enzymes ; *Genes ; Genetic Code ; Humans ; Models, Molecular ; Nucleic Acid Hybridization ; Rats ; Receptors, Muscarinic/classification/*genetics ; Swine ; Transfection
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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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    Three-dimensional structure of interleukin-2 (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-18
    Description: Interleukin-2 is an effector protein that participates in modulating the immune response; it has become a focal point for the study of lymphokine structure and function. The three-dimensional structure of the interleukin molecule has been solved to 3.0 angstrom resolution. Interleukin-2 has a novel alpha-helical tertiary structure that suggests one portion of the molecule forms a structural scaffold, which underlies the receptor binding facets of the molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brandhuber, B J -- Boone, T -- Kenney, W C -- McKay, D B -- A1-00631/PHS HHS/ -- A1-19762/PHS HHS/ -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1707-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3500515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Interleukin-2/isolation & purification ; Mice ; Models, Molecular ; Protein Conformation ; Solvents ; X-Ray Diffraction
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  • 7
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    Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-08
    Description: beta-lactamases are enzymes that protect bacteria from the lethal effects of beta-lactam antibiotics, and are therefore of considerable clinical importance. The crystal structure of beta-lactamase from the Gram-positive bacterium Staphylococcus aureus PC1 has been determined at 2.5 angstrom resolution. It reveals a molecule of novel topology, made up of two closely associated domains. The active site is located at the interface between the domains, with the key catalytic residue Ser70 at the amino terminus of a buried helix. Examination of the disposition of the functionally important residues within the active site depression leads to a model for the binding of a substrate and a functional analogy to the serine proteases. The unusual topology of the secondary structure units is relevant to questions concerning the evolutionary relation to the beta-lactam target enzymes of the bacterial cell wall.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzberg, O -- Moult, J -- New York, N.Y. -- Science. 1987 May 8;236(4802):694-701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107125" target="_blank"〉PubMed〈/a〉
    Keywords: *Anti-Bacterial Agents/metabolism ; Binding Sites ; Biological Evolution ; Catalysis ; Crystallization ; Drug Resistance, Microbial ; Endopeptidases ; Models, Molecular ; Polyethylene Glycols ; Protein Conformation ; Serine ; Serine Endopeptidases ; Solvents ; Staphylococcus aureus/*enzymology ; *beta-Lactamases/metabolism ; beta-Lactams
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  • 8
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    Epitope mapping by chemical modification of free and antibody-bound protein antigen (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-02-13
    Description: A monoclonal antibody bound to a protein antigen slows the rate of chemical modification of amino acid residues located at the epitope. By comparing the degree of acetylation of 18 lysine and 7 threonine residues in free and antibody-bound horse cytochrome c, a discontiguous, conformational epitope was characterized on this protein antigen. The new approach is particularly suitable to probe discontiguous and conformational epitopes, which are difficult to analyze by other procedures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burnens, A -- Demotz, S -- Corradin, G -- Binz, H -- Bosshard, H R -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):780-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2433768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology ; *Antigen-Antibody Complex ; Cytochrome c Group/*immunology ; Epitopes/*immunology ; Horses ; Humans ; Models, Molecular ; Protein Conformation ; Species Specificity
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  • 9
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    Isolation and structure of a covalent cross-link adduct between mitomycin C and DNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-06
    Description: A DNA cross-link adduct of the antitumor agent mitomycin C (MC) to DNA has been isolated and characterized; the results provide direct proof for bifunctional alkylation of DNA by MC. Exposure of MC to Micrococcus luteus DNA under reductive conditions and subsequent nuclease digestion yielded adducts formed between MC and deoxyguanosine residues. In addition to the two known monoadducts, a bisadduct was obtained. Reductive MC activation with Na2S2O4 (sodium dithionite) leads to exclusive bifunctional alkylation. The structure of the bisadduct was determined by spectroscopic methods that included proton magnetic resonance, differential Fourier transform infrared spectroscopy, and circular dichroism. Formation of the same bisadduct in vivo was demonstrated upon injection of rats with MC. Computer-generated models of the bisadduct that was incorporated into the center of the duplex B-DNA decamer d(CGTACGTACG)2 indicated that the bisadduct fit snugly into the minor groove with minimal distortion of DNA structure. A mechanistic analysis of the factors that govern monofunctional and bifunctional adduct formation is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomasz, M -- Lipman, R -- Chowdary, D -- Pawlak, J -- Verdine, G L -- Nakanishi, K -- CA 11572/CA/NCI NIH HHS/ -- CA 28681/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 6;235(4793):1204-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3103215" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Cross-Linking Reagents/*isolation & purification ; DNA/*metabolism ; Mass Spectrometry ; Mitomycin ; Mitomycins/*metabolism ; Models, Molecular
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  • 10
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    Structure of a psoralen cross-linked DNA in solution by nuclear magnetic resonance (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-18
    Description: One- and two-dimensional nuclear magnetic resonance (NMR) methods were used to determine a three-dimensional model of an eight-base-pair DNA fragment (d-GGGTACCC) cross-linked with psoralen in solution. Two-dimensional nuclear Overhauser effect experiments were used to assign the spectrum and estimate distances for 171 proton pairs in the cross-linked DNA. The NMR-derived model shows a 53 degree bend into the major groove that occurs primarily at the site of drug addition and a 56 degree unwinding that spans the eight-base-pair duplex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomic, M T -- Wemmer, D E -- Kim, S H -- GM 31616/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1722-5.〈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/3686011" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; *Cross-Linking Reagents ; *Dna ; Magnetic Resonance Spectroscopy/methods ; *Methoxsalen ; Models, Molecular ; Nucleic Acid Conformation ; *Oligodeoxyribonucleotides ; *Thymine
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  • 11
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    Molecular dynamics of a cytochrome c-cytochrome b5 electron transfer complex (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-06
    Description: Cytochrome c and cytochrome b5 form an electrostatically associated electron transfer complex. Computer models of this and related complexes that were generated by docking the x-ray structures of the individual proteins have provided insight into the specificity and mechanism of electron transfer reactions. Previous static modeling studies were extended by molecular dynamics simulations of a cytochrome c-cytochrome b5 intermolecular complex. The simulations indicate that electrostatic interactions at the molecular interface results in a flexible association complex that samples alternative interheme geometries and molecular conformations. Many of these transient geometries appear to be more favorable for electron transfer than those formed in the initial model complex. Of particular interest is a conformational change that occurred in phenylalanine 82 of cytochrome c that allowed the phenyl side chain to bridge the two cytochrome heme groups.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wendoloski, J J -- Matthew, J B -- Weber, P C -- Salemme, F R -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):794-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research and Development Department, E. I. du Pont de Nemours and Company, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2823387" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Graphics ; Cytochrome b Group/*metabolism ; Cytochrome c Group/*metabolism ; Cytochromes b5 ; Electron Transport ; Kinetics ; Models, Molecular ; Protein Binding ; Protein Conformation
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  • 12
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    Engineering enzyme specificity by "substrate-assisted catalysis" (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-24
    Description: A novel approach to engineering enzyme specificity is presented in which a catalytic group from an enzyme is first removed by site-directed mutagenesis causing inactivation. Activity is then partially restored by substrates containing the missing catalytic functional group. Replacement of the catalytic His with Ala in the Bacillus amyloliquefaciens subtilisin gene (the mutant is designated His64Ala) by site-directed mutagenesis reduces the catalytic efficiency (kcat/Km) by a factor of a million when assayed with N-succinyl-L-Phe-L-Ala-L-Ala-L-Phe-p-nitroanilide (sFAAF-pNA). Model building studies showed that a His side chain at the P2 position of a substrate bound at the active site of subtilisin could be virtually superimposed on the catalytic His side chain of this serine protease. Accordingly, the His64Ala mutant hydrolyzes a His P2 substrate (sFAHF-pNA) up to 400 times faster than a homologous Ala P2 or Gln P2 substrate (sFAAF-pNA or sFAQF-pNA) at pH 8.0. In contrast, the wild-type enzyme hydrolyzes these three substrates with similar catalytic efficiencies. Additional data from substrate-dependent pH profiles and hydrolysis of large polypeptides indicate that the His64Ala mutant enzyme can recover partially the function of the lost catalytic histidine from a His P2 side chain on the substrate. Such "substrate-assisted catalysis" provides a new basis for engineering enzymes with very narrow and potentially useful substrate specificities. These studies also suggest a possible functional intermediate in the evolution of the catalytic triad of serine proteases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, P -- Wells, J A -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):394-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299704" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Enzymes/*metabolism ; Models, Molecular ; Molecular Conformation ; Mutation ; Protein Binding ; Protein Conformation ; Substrate Specificity ; Subtilisins/genetics/*metabolism
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  • 13
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    Atomic structure of thymidylate synthase: target for rational drug design (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-01-23
    Description: The atomic structure of thymidylate synthase from Lactobacillus casei was determined at 3 angstrom resolution. The native enzyme is a dimer of identical subunits. The dimer interface is formed by an unusual association between five-stranded beta sheets present in each monomer. Comparison of known sequences with the Lactobacillus casei structure suggests that they all have a common core structure around which loops are inserted or deleted in different sequences. Residues from both subunits contribute to each active site. Two arginine side chains can contribute to binding phosphate on the substrate. The side chains of several conserved amino acids can account for other determinants of substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardy, L W -- Finer-Moore, J S -- Montfort, W R -- Jones, M O -- Santi, D V -- Stroud, R M -- AI 19358/AI/NIAID NIH HHS/ -- CA41323/CA/NCI NIH HHS/ -- GM 24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 23;235(4787):448-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3099389" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography ; Deoxyuracil Nucleotides/metabolism ; Lactobacillus casei/enzymology ; Models, Molecular ; Protein Conformation ; Structure-Activity Relationship ; *Thymidylate Synthase/antagonists & inhibitors
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  • 14
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    A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-15
    Description: A better understanding of the molecular mechanism of protein biosynthesis depends on the availability of a reliable model for the ribosome particle. The application of a diffraction technique, namely, three-dimensional image reconstruction from two-dimensional sheets of the large ribosomal subunits of Bacillus stearothermophilus at a resolution of 30 angstroms is described. The resulting three-dimensional model shows at least four projecting arms, arranged radially near the presumed interface with the 30S subunit. The projecting arms are positioned around a cleft, which turns into a tunnel with a length of 100 to 120 angstroms and a diameter of up to 25 angstroms. This tunnel spans the particle and may provide the path taken by the nascent polypeptide chain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yonath, A -- Leonard, K R -- Wittmann, H G -- GM34360/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 15;236(4803):813-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576200" target="_blank"〉PubMed〈/a〉
    Keywords: Geobacillus stearothermophilus/*ultrastructure ; Microscopy, Electron ; Models, Molecular ; Ribosomes/*ultrastructure
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