Motifs involved in protein-protein interactions
Identifieur interne : 001C47 ( Istex/Checkpoint ); précédent : 001C46; suivant : 001C48Motifs involved in protein-protein interactions
Auteurs : C. Slingsby [Royaume-Uni] ; O. A. Bateman [Royaume-Uni] ; A. Simpson [Royaume-Uni]Source :
- Molecular Biology Reports [ 0301-4851 ] ; 1993-04-01.
English descriptors
- KwdEn :
- Teeft :
- Amino acids, Antiparallel strands, Barrel axes, Biol, Catalytic domain, Constant domains, Crystal structure, Cubic symmetry, Different orientation, Different subunits, Dihydrolipoyl transacetylase, Dimer, Dimer axis, Dimer formation, Dimer interface, Domain, Edge strands, Extracellular domain, First helix, Helix, Helix bundle, Helix bundles, Human growth hormone, Human growth hormone receptor, Hydrophobic side chains, Identical subunits, Immunoglobulin, Interface, Interface interactions, Intermolecular contacts, Linker region, Long axes, Long loop, Loop regions, Monomer, Oligomer, Polypeptide, Protein domains, Protein structure, Protein structures, Pseudo axis, Receptor, Rotation axis, Sandwich structure, Strand, Subunit, Symmetrical assemblies, Tandem domains, Topology, Trends biochem, Twofold axis, Variable domains.
Abstract
Summary: Interactions between proteins are extremely variable. However, in the dimeric proteins comprised of regular motifs, interface interactions are similar to those that stabilize monomers. Additional stability is gained by converting loops within motifs or domains to linkers across interfaces. In multi-domain proteins, interactions can be greatly effected by the conformation of linkers between domains. Complex association of subunits, involving higher rotational symmetry or cubic symmetry, frequently involves motif sharing across interfaces.
Url:
DOI: 10.1007/BF00986727
Affiliations:
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ISTEX:EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7Le document en format XML
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Simpson</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7</idno><date when="1993" year="1993">1993</date><idno type="doi">10.1007/BF00986727</idno><idno type="url">https://api.istex.fr/ark:/67375/1BB-7H7030FS-6/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001178</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001178</idno><idno type="wicri:Area/Istex/Curation">001178</idno><idno type="wicri:Area/Istex/Checkpoint">001C47</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001C47</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Motifs involved in protein-protein interactions</title><author><name sortKey="Slingsby, C" sort="Slingsby, C" uniqKey="Slingsby C" first="C." last="Slingsby">C. Slingsby</name><affiliation wicri:level="3"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London</wicri:regionArea><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author><author><name sortKey="Bateman, O A" sort="Bateman, O A" uniqKey="Bateman O" first="O. A." last="Bateman">O. A. Bateman</name><affiliation wicri:level="3"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London</wicri:regionArea><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author><author><name sortKey="Simpson, A" sort="Simpson, A" uniqKey="Simpson A" first="A." last="Simpson">A. Simpson</name><affiliation wicri:level="3"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London</wicri:regionArea><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Biology Reports</title><title level="j" type="sub">An International Journal on Molecular and Cellular Biology</title><title level="j" type="abbrev">Mol Biol Rep</title><idno type="ISSN">0301-4851</idno><idno type="eISSN">1573-4978</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="1993-04-01">1993-04-01</date><biblScope unit="volume">17</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="185">185</biblScope><biblScope unit="page" to="195">195</biblScope></imprint><idno type="ISSN">0301-4851</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0301-4851</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>domain</term><term>helix-bundle</term><term>interface</term><term>motif</term><term>oligomer</term><term>β-sheet</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Amino acids</term><term>Antiparallel strands</term><term>Barrel axes</term><term>Biol</term><term>Catalytic domain</term><term>Constant domains</term><term>Crystal structure</term><term>Cubic symmetry</term><term>Different orientation</term><term>Different subunits</term><term>Dihydrolipoyl transacetylase</term><term>Dimer</term><term>Dimer axis</term><term>Dimer formation</term><term>Dimer interface</term><term>Domain</term><term>Edge strands</term><term>Extracellular domain</term><term>First helix</term><term>Helix</term><term>Helix bundle</term><term>Helix bundles</term><term>Human growth hormone</term><term>Human growth hormone receptor</term><term>Hydrophobic side chains</term><term>Identical subunits</term><term>Immunoglobulin</term><term>Interface</term><term>Interface interactions</term><term>Intermolecular contacts</term><term>Linker region</term><term>Long axes</term><term>Long loop</term><term>Loop regions</term><term>Monomer</term><term>Oligomer</term><term>Polypeptide</term><term>Protein domains</term><term>Protein structure</term><term>Protein structures</term><term>Pseudo axis</term><term>Receptor</term><term>Rotation axis</term><term>Sandwich structure</term><term>Strand</term><term>Subunit</term><term>Symmetrical assemblies</term><term>Tandem domains</term><term>Topology</term><term>Trends biochem</term><term>Twofold axis</term><term>Variable domains</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Summary: Interactions between proteins are extremely variable. However, in the dimeric proteins comprised of regular motifs, interface interactions are similar to those that stabilize monomers. Additional stability is gained by converting loops within motifs or domains to linkers across interfaces. In multi-domain proteins, interactions can be greatly effected by the conformation of linkers between domains. Complex association of subunits, involving higher rotational symmetry or cubic symmetry, frequently involves motif sharing across interfaces.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Grand Londres</li></region><settlement><li>Londres</li></settlement></list><tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Slingsby, C" sort="Slingsby, C" uniqKey="Slingsby C" first="C." last="Slingsby">C. Slingsby</name></region><name sortKey="Bateman, O A" sort="Bateman, O A" uniqKey="Bateman O" first="O. A." last="Bateman">O. A. Bateman</name><name sortKey="Simpson, A" sort="Simpson, A" uniqKey="Simpson A" first="A." last="Simpson">A. Simpson</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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