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  • Articles  (20)
  • Latest Papers from Table of Contents or Articles in Press  (20)
  • Protein Conformation
  • 2000-2004
  • 1985-1989  (20)
  • 1935-1939
  • 1986  (20)
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  • Articles  (20)
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  • Latest Papers from Table of Contents or Articles in Press  (20)
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  • 2000-2004
  • 1985-1989  (20)
  • 1935-1939
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  • 1
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    Three-dimensional structure of favin: saccharide binding-cyclic permutation in leguminous lectins (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-28
    Description: The three-dimensional structure of favin, the glucose- and mannose-binding lectin of Vicia faba (vetch, broad bean), has been determined at a resolution of 2.8 angstroms by molecular replacement. The crystals contain specifically bound glucose and provide the first high-resolution view of specific saccharide binding in a leguminous lectin. The structure is similar to those of concanavalin A (Con A) and green pea lectin; differences from Con A show that minimal changes are needed to accommodate the cyclic permutation in amino acid sequence between the two molecules. The molecule is an ellipsoidal dimer dominated by extensive beta structures. Each protomer contains binding sites for two divalent metal ions (Mn2+ and Ca2+) and a specific saccharide. Glucose is bound by favin in a cleft in the molecular surface and has noncovalent contacts primarily with two peptide loops, one of which contains several metal ion ligands. The specific carbohydrate-binding site is similar to that of Con A in location and general peptide folding, despite several differences in specific amino acid residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reeke, G N Jr -- Becker, J W -- AI-11378/AI/NIAID NIH HHS/ -- GM-22663/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 28;234(4780):1108-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775378" target="_blank"〉PubMed〈/a〉
    Keywords: Concanavalin A ; *Lectins ; Plant Lectins ; Plants ; Protein Conformation
    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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  • 2
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    Structural heterogeneity and functional domains of murine immunoglobulin G Fc receptors (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-07
    Description: Binding of antibodies to effector cells by way of receptors to their constant regions (Fc receptors) is central to the pathway that leads to clearance of antigens by the immune system. The structure and function of this important class of receptors on immune cells is addressed through the molecular characterization of Fc receptors (FcR) specific for the murine immunoglobulin G isotype. Structural diversity is encoded by two genes that by alternative splicing result in expression of molecules with highly conserved extracellular domains and different transmembrane and intracytoplasmic domains. The proteins encoded by these genes are members of the immunoglobulin supergene family, most homologous to the major histocompatibility complex molecule E beta. Functional reconstitution of ligand binding by transfection of individual FcR genes demonstrates that the requirements for ligand binding are encoded in a single gene. These studies demonstrate the molecular basis for the functional heterogeneity of FcR's, accounting for the possible transduction of different signals in response to a single ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravetch, J V -- Luster, A D -- Weinshank, R -- Kochan, J -- Pavlovec, A -- Portnoy, D A -- Hulmes, J -- Pan, Y C -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- GM 36306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):718-25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2946078" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/genetics ; Gene Expression Regulation ; Histocompatibility Antigens Class II/genetics ; Immunoglobulin G ; Lymphocytes/*physiology ; Macrophages/*physiology ; Membrane Proteins ; Mice ; Protein Conformation ; *Receptors, Fc/genetics ; Receptors, IgG ; Transcription, Genetic ; Transfection
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  • 3
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    A genetic approach to analyzing membrane protein topology (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-09-26
    Description: Fusions of the secreted protein alkaline phosphatase to an integral cytoplasmic membrane protein of Escherichia coli showed different activities depending on where in the membrane protein the alkaline phosphatase was fused. Fusions to positions in or near the periplasmic domain led to high alkaline phosphatase activity, whereas those to positions in the cytoplasmic domain gave low activity. Analysis of alkaline phosphatase fusions to membrane proteins of unknown structure may thus be generally useful in determining their membrane topologies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manoil, C -- Beckwith, J -- New York, N.Y. -- Science. 1986 Sep 26;233(4771):1403-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3529391" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaline Phosphatase/genetics ; Cell Membrane/ultrastructure ; Chromosome Deletion ; Escherichia coli/genetics ; Membrane Proteins/*genetics ; Mutation ; Plasmids ; Protein Conformation ; Recombinant Proteins/analysis
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  • 4
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    Crystal structure analysis of deamino-oxytocin: conformational flexibility and receptor binding (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-02
    Description: Two crystal structures of deamino-oxytocin have been determined at better than 1.1A resolution from isomorphous replacement and anomalous scattering x-ray measurements. In each of two crystal forms there are two closely related conformers with disulfide bridges of different chirality, which may be important in receptor recognition and activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wood, S P -- Tickle, I J -- Treharne, A M -- Pitts, J E -- Mascarenhas, Y -- Li, J Y -- Husain, J -- Cooper, S -- Blundell, T L -- Hruby, V J -- AM-10080/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 May 2;232(4750):633-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Dimethyl Sulfoxide ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Oxytocin/*analogs & derivatives/metabolism ; Protein Conformation ; Receptors, Angiotensin/*metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Oxytocin ; X-Ray Diffraction
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  • 5
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    Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray crystallographic techniques. No conformational changes can be observed in the tertiary structure of lysozyme compared with that determined in native crystalline forms. The quaternary structure of Fab is that of an extended conformation. The antibody combining site is a rather flat surface with protuberances and depressions formed by its amino acid side chains. The antigen-antibody interface is tightly packed, with 16 lysozyme and 17 antibody residues making close contacts. The antigen contacting residues belong to two stretches of the lysozyme polypeptide chain: residues 18 to 27 and 116 to 129. All the complementarity-determining regions and two residues outside hypervariable positions of the antibody make contact with the antigen. Most of these contacts (10 residues out of 17) are made by the heavy chain, and in particular by its third complementarity-determining region. Antigen variability and antibody specificity and affinity are discussed on the basis of the determined structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amit, A G -- Mariuzza, R A -- Phillips, S E -- Poljak, R J -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):747-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2426778" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Monoclonal ; *Antigen-Antibody Complex ; Chickens ; Egg White ; Epitopes ; *Immunoglobulin Fab Fragments ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; In Vitro Techniques ; Kinetics ; Models, Molecular ; Muramidase/*immunology ; Protein Conformation ; X-Ray Diffraction
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  • 6
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    Two-dimensional nuclear magnetic resonance spectroscopy (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-23
    Description: Great spectral simplification can be obtained by spreading the conventional one-dimensional nuclear magnetic resonance (NMR) spectrum in two independent frequency dimensions. This so-called two-dimensional NMR spectroscopy removes spectral overlap, facilitates spectral assignment, and provides a wealth of additional information. For example, conformational information related to interproton distances is available from resonance intensities in certain types of two-dimensional experiments. Another method generates 1H NMR spectra of a preselected fragment of the molecule, suppressing resonances from other regions and greatly simplifying spectral appearance. Two-dimensional NMR spectroscopy can also be applied to the study of 13C and 15N, not only providing valuable connectivity information but also improving sensitivity of 13C and 15N detection by up to two orders of magnitude.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bax, A -- Lerner, L -- New York, N.Y. -- Science. 1986 May 23;232(4753):960-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3518060" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon ; Hydrogen ; Magnetic Resonance Spectroscopy/*methods ; Muramidase ; Nitrogen ; Nucleic Acid Conformation ; Oligoribonucleotides ; Operator Regions, Genetic ; Protein Conformation
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  • 7
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    Conformations of signal peptides induced by lipids suggest initial steps in protein export (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-07-11
    Description: Despite the requirement for a functional signal sequence in protein export, little is known of the conformational properties and membrane interactions of these highly hydrophobic amino terminal extensions on nearly all exported proteins. The Escherichia coli lambda phage receptor signal sequence was studied in phospholipid monolayers by circular dichroism and Fourier transform infrared spectroscopy; the signal peptide was shown to prefer an alpha-helical conformation when inserted into the lipid phase. However, interaction with the lipid surface without insertion induced the signal sequence, which is unstructured in bulk aqueous solution, to adopt a beta structure. These observations are combined in a model for the initial steps in signal sequence-membrane interaction in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Briggs, M S -- Cornell, D G -- Dluhy, R A -- Gierasch, L M -- GM-34962/GM/NIGMS NIH HHS/ -- RR-01367/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):206-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2941862" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/metabolism ; Cell Membrane/metabolism ; Circular Dichroism ; Membrane Lipids/metabolism/*physiology ; Phospholipids/metabolism ; Protein Conformation ; Protein Sorting Signals/*physiology ; Proteins/*secretion ; Spectrophotometry, Infrared
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  • 8
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    Multiple DNA-protein interactions governing high-precision DNA transactions (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-09-05
    Description: The precise association of DNA-binding proteins with localized regions of DNA is crucial for regulated replication and expression of the genome. For certain DNA transactions, the requirement for precision in localization and control is extremely high. High-precision events amenable to detailed biochemical analysis are the initiation of DNA replication and site-specific recombination by bacteriophage lambda and Escherichia coli. Recent experiments indicate that site-localization and control in these reactions involves the association of DNA-bound proteins to generate organized nucleoprotein structures in which the DNA is folded or wound. These specialized nucleoprotein structures are likely to provide the requisite accuracy for site localization and the necessary regulated reactivity to direct the DNA transaction. Multiple DNA-protein interactions are also required for controlled transcription of the eukaryotic genome. Distant upstream regulator and enhancer sequences may define protein-binding sites that form part of a reactive nucleoprotein structure capable of initiating transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Echols, H -- GM17078/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 5;233(4768):1050-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2943018" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/physiology ; Bacteriophage lambda/*genetics ; *DNA Replication ; DNA-Binding Proteins/*physiology ; Enhancer Elements, Genetic ; Escherichia coli/*genetics ; Macromolecular Substances ; Microscopy, Electron ; Nucleic Acid Conformation ; Nucleoproteins/*physiology ; Promoter Regions, Genetic ; Protein Conformation ; *Recombination, Genetic ; Transcription Factors/*physiology ; Viral Proteins/physiology
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  • 9
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    On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-21
    Description: Structural data are now available for comparing a penicillin target enzyme, the D-alanyl-D-alanine-peptidase from Streptomyces R61, with a penicillin-hydrolyzing enzyme, the beta-lactamase from Bacillus licheniformis 749/C. Although the two enzymes have distinct catalytic properties and lack relatedness in their overall amino acid sequences except near the active-site serine, the significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Dideberg, O -- Charlier, P -- Wery, J P -- Libert, M -- Moews, P C -- Knox, J R -- Duez, C -- Fraipont, C -- Joris, B -- 10RRO1955-01/RR/NCRR NIH HHS/ -- AI-10925/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 21;231(4744):1429-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3082007" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillus cereus/enzymology ; Binding Sites ; Carboxypeptidases/genetics/*metabolism ; Molecular Weight ; *Penicillin Resistance ; Protein Conformation ; *Serine-Type D-Ala-D-Ala Carboxypeptidase ; Streptomyces/enzymology ; X-Ray Diffraction ; beta-Lactamases/genetics/*metabolism
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  • 10
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    Active human-yeast chimeric phosphoglycerate kinases engineered by domain interchange (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: Phosphoglycerate kinase (PGK) is a monomeric protein composed of two domains of approximately equal size, connected by a hinge. Substrate-induced conformational change results in the closure of the active site cleft, which is situated between these two domains. In a study of the relations between structure and function of this enzyme, two interspecies hybrids were constructed, each composed of one domain from the human enzyme and one domain from the yeast enzyme. Despite a 35% difference in the amino acid composition between human and yeast PGK, catalytic properties of the hybrid enzymes are very similar to those of the parental proteins. This result demonstrates that the evolutionary substitutions within these two distantly related molecules do not significantly affect formation of the active site cleft, mechanism of domain closure, or enzyme activity itself.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mas, M T -- Chen, C Y -- Hitzeman, R A -- Riggs, A D -- R01 GM31263/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):788-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526552" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; *Chimera ; *Genes ; *Genes, Fungal ; Genetic Engineering ; Humans ; Kinetics ; Models, Molecular ; Phosphoglycerate Kinase/*genetics/metabolism ; Plasmids ; Protein Conformation ; Protein Multimerization ; Saccharomyces cerevisiae/enzymology/*genetics
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  • 11
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    The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-09
    Description: The crystalline complex of pancreatic ribonuclease (RNase) with oligomers of d(pA)4 has been solved by x-ray diffraction methods and refined by standard procedures to a conventional crystallographic R factor of 0.22 at 2.5 angstrom resolution. The asymmetric unit is a complex of one RNase molecule associated with four d(pA)4 oligomers. Although the DNA in this complex is segmented, and therefore shows some discontinuities, it nevertheless traces a continuous path 12 nucleotides in length that passes through the active site cleft of the enzyme and over the surface of the protein. The DNA makes a series of eight to nine electrostatic bonds between its phosphate groups and lysine and arginine residues on the protein, as well as specific chemical interactions at the active site. The path described by the sequence of nucleotides is likely to be that taken by an extended polynucleotide chain when it is bound by the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McPherson, A -- Brayer, G -- Cascio, D -- Williams, R -- 21398/PHS HHS/ -- New York, N.Y. -- Science. 1986 May 9;232(4751):765-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961503" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; DNA/metabolism ; Models, Molecular ; Polynucleotides/metabolism ; Protein Conformation ; Ribonuclease, Pancreatic/*metabolism ; X-Ray Diffraction
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  • 12
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    Three-dimensional structure of the adenovirus major coat protein hexon (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-30
    Description: The three-dimensional crystal structure of the adenovirus major coat protein is presented. Adenovirus type 2 hexon, at 967 residues, is now the longest polypeptide whose structure has been determined crystallographically. Taken with our model for hexon packing, which positions the 240 trimeric hexons in the capsid, the structure defines 60% of the protein within the 150 X 10(6) dalton virion. The assembly provides the first details of a DNA-containing animal virus that is 20 times larger than the spherical RNA viruses previously described. Unexpectedly, the hexon subunit contains two similar beta-barrels whose topology is identical to those of the spherical RNA viruses, but whose architectural role in adenovirus is very different. The hexon structure reveals several distinctive features related to its function as a stable protective coat, and shows that the type-specific immunological determinants are restricted to the virion surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, M M -- White, J L -- Grutter, M G -- Burnett, R M -- AI 17270/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 May 30;232(4754):1148-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3704642" target="_blank"〉PubMed〈/a〉
    Keywords: *Adenoviridae/genetics/ultrastructure ; Amino Acid Sequence ; *Capsid/genetics/ultrastructure ; *Capsid Proteins ; Protein Conformation ; RNA Viruses/ultrastructure ; X-Ray Diffraction
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  • 13
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    Structure of the DNA-Eco RI endonuclease recognition complex at 3 A resolution (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: The crystal structure of the complex between Eco RI endonuclease and the cognate oligonucleotide TCGCGAATTCGCG provides a detailed example of the structural basis of sequence-specific DNA-protein interactions. The structure was determined, to 3 A resolution, by the ISIR (iterative single isomorphous replacement) method with a platinum isomorphous derivative. The complex has twofold symmetry. Each subunit of the endonuclease is organized into an alpha/beta domain consisting a five-stranded beta sheet, alpha helices, and an extension, called the "arm," which wraps around the DNA. The large beta sheet consists of antiparallel and parallel motifs that form the foundations for the loops and alpha helices responsible for DNA strand scission and sequence-specific recognition, respectively. The DNA cleavage site is located in a cleft that binds the DNA backbone in the vicinity of the scissile bond. Sequence specificity is mediated by 12 hydrogen bonds originating from alpha helical recognition modules. Arg200 forms two hydrogen bonds with guanine while Glu144 and Arg145 form four hydrogen bonds to adjacent adenine residues. These interactions discriminate the Eco RI hexanucleotide GAATTC from all other hexanucleotides because any base substitution would require rupture of at least one of these hydrogen bonds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McClarin, J A -- Frederick, C A -- Wang, B C -- Greene, P -- Boyer, H W -- Grable, J -- Rosenberg, J M -- GM25671/GM/NIGMS NIH HHS/ -- GM33506/GM/NIGMS NIH HHS/ -- RR07084/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1526-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3024321" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/metabolism ; Base Composition ; Binding Sites ; Chemistry, Physical ; Crystallization ; DNA/*metabolism ; DNA Restriction Enzymes/*metabolism ; Deoxyribonuclease EcoRI ; Hydrogen Bonding ; Macromolecular Substances ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/metabolism ; Physicochemical Phenomena ; Protein Conformation ; Substrate Specificity
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  • 14
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    The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: Predictions of the structures of the antigen-binding domains of an antibody, recorded before its experimental structure determination and tested subsequently, were based on comparative analysis of known antibody structures or on conformational energy calculations. The framework, the relative positions of the hypervariable regions, and the folds of four of the hypervariable loops were predicted correctly. This portion includes all residues in contact with the antigen, in this case hen egg white lysozyme, implying that the main chain conformation of the antibody combining site does not change upon ligation. The conformations of three residues in each of the other two hypervariable loops are different in the predicted models and the experimental structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chothia, C -- Lesk, A M -- Levitt, M -- Amit, A G -- Mariuzza, R A -- Phillips, S E -- Poljak, R J -- GM25435/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):755-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3090684" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; *Antigen-Antibody Complex ; Chickens ; Egg White ; Female ; Immunoglobulin Fab Fragments ; *Immunoglobulin G ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; Immunoglobulin Variable Region ; Models, Molecular ; Muramidase/immunology ; Protein Conformation
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  • 15
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    Automated chemical synthesis of a protein growth factor for hemopoietic cells, interleukin-3 (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-10
    Description: Interleukin-3 (IL-3), a protein of 140 amino acids, was chemically synthesized by means of an automated peptide synthesizer and was shown to have the biological activities attributed to native IL-3. Assays of synthetic analogues established that an amino terminal fragment has detectable IL-3 activity, but that the stable tertiary structure of the complete molecule was required for full activity. The results demonstrate that automated peptide synthesis can be applied to the study of the structure and function of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark-Lewis, I -- Aebersold, R -- Ziltener, H -- Schrader, J W -- Hood, L E -- Kent, S B -- R01-CA38684-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):134-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079915" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Chromatography, High Pressure Liquid ; Electrophoresis, Polyacrylamide Gel ; Interleukin-3 ; Lymphokines/*chemical synthesis/pharmacology ; Mast Cells/drug effects ; Megakaryocytes/drug effects ; Mice ; Protein Conformation ; Structure-Activity Relationship
    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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  • 16
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    Protein, DNA, and virus crystallography with a focused imaging proportional counter (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-30
    Description: A set of programs has been developed for rapid collection of x-ray intensity data from protein and virus crystals with a commercially available two-dimensional focused geometry electronic detector. The detector is compact and portable, with unusually high spatial resolution comparable to that used in oscillation photography. It has allowed x-ray data collection on weakly diffracting crystals with large unit cells, as well as more conventional "diffractometer-quality" crystals. The quality of the data is compared with that from oscillation photography and automated diffractometry in the range of unit cells from 96.3 to 383.2 angstroms. Isomorphous and anomalous difference Pattersons, based on detector data, are shown for a variable surface glycoprotein mercury derivative and for a repressor-DNA bromine derivative, which has been solved at 7 angstroms with detector data only.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Durbin, R M -- Burns, R -- Moulai, J -- Metcalf, P -- Freymann, D -- Blum, M -- Anderson, J E -- Harrison, S C -- Wiley, D C -- AI13654/AI/NIAID NIH HHS/ -- CA13202/CA/NCI NIH HHS/ -- GM29109/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 May 30;232(4754):1127-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3704639" target="_blank"〉PubMed〈/a〉
    Keywords: Computers ; *Dna ; Mathematics ; Nucleic Acid Conformation ; Protein Conformation ; *Proteins ; Viruses/*ultrastructure ; X-Ray Diffraction/instrumentation/*methods
    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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  • 17
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    Crystal structure of Cd,Zn metallothionein (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-02-14
    Description: The anomalous scattering data from five Cd in the native protein were used to determine the crystal structure of cadmium, zinc (Cd,Zn) metallothionein isoform II from rat liver. The structure of a 4-Cd cluster was solved by direct methods. A 2.3 A resolution electron density map was calculated by iterative single-wavelength anomalous scattering. The structure is folded into two domains. The amino terminal domain (beta) of residues 1 to 29 enfolds a three-metal cluster of one Cd and two Zn atoms coordinated by six terminal cysteine thiolate ligands and three bridging cysteine thiolates. The carboxyl terminal domain (alpha) of residues 30 to 61 enfolds a 4-Cd cluster coordinated by six terminal and five bridging cysteine thiolates. All seven metal sites have tetrahedral coordination geometry. The domains are roughly spherical, and the diameter is 15 to 20 A; there is limited contact between domains. The folding of alpha and beta is topologically similar but with opposite chirality. Redundant, short cysteine-containing sequences have similar roles in cluster formation in both alpha and beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Furey, W F -- Robbins, A H -- Clancy, L L -- Winge, D R -- Wang, B C -- Stout, C D -- GM-36535/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Feb 14;231(4739):704-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3945804" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cadmium ; Crystallography ; Cysteine ; *Metallothionein ; Models, Molecular ; Protein Conformation ; Rats ; Solutions ; X-Ray Diffraction ; Zinc
    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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  • 18
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    Mapping epitopes on a protein antigen by the proteolysis of antigen-antibody complexes (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-23
    Description: A monoclonal antibody bound to a protein antigen decreases the rate of proteolytic cleavage of the antigen, having the greatest effect on those regions involved in antibody contact. Thus, an epitope can be identified by the ability of the antibody to protect one region of the antigen more than others from proteolysis. By means of this approach, two distinct epitopes, both conformationally well-ordered, were characterized on horse cytochrome c.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jemmerson, R -- Paterson, Y -- AI 19499/AI/NIAID NIH HHS/ -- AI21486/AI/NIAID NIH HHS/ -- GM 31841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 May 23;232(4753):1001-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2422757" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; *Antigen-Antibody Complex ; Cytochrome c Group/*immunology ; *Epitopes ; Mice ; Oligopeptides/immunology ; Protein Conformation ; Trypsin
    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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  • 19
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    Reversible interconversion of two forms of a valyl-tRNA synthetase-containing protein complex (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-28
    Description: When an enzyme-containing complex from yeast was incubated in a buffered solution at room temperature, the valyl-transfer RNA synthetase activity and total protein oscillated synchronously between two physical states. This observation suggests a regulatory process that controls a number of enzymes as a group, an integrated function of a kind not heretofore recognized. The two forms of the complex were separated by ammonium sulfate precipitation of one of them in samples withdrawn from the incubated solution every 30 seconds. Glutathione and dithiothreitol in high concentrations (50 mM) enhance formation of the 50% saturated ammonium sulfate-soluble form. Oxidized glutathione, diphosphopyridine nucleotide, triphosphopyridine nucleotide, and a mercurial thiol binding agent in moderate concentrations (0.1 to 1.0 mM) shift the distribution toward the precipitable form. It is suggested that the two forms represent functional and nonfunctional complex-bound enzymes which are interconverted in response to oxidoreductive signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Black, S -- New York, N.Y. -- Science. 1986 Nov 28;234(4780):1111-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3535073" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acyl-tRNA Synthetases/*metabolism ; Dithiothreitol/metabolism ; Glutathione/metabolism ; Macromolecular Substances ; NAD/metabolism ; NADP/metabolism ; Protein Conformation ; Saccharomyces cerevisiae/enzymology ; Valine-tRNA Ligase/*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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  • 20
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    Structural basis for antigen-antibody recognition (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, R -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):702-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2426777" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen-Antibody Complex ; Epitopes ; Immunoglobulin Fab Fragments ; Models, Molecular ; Muramidase ; Protein Conformation
    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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