Motifs involved in protein-protein interactions
Identifieur interne : 001178 ( Istex/Corpus ); précédent : 001177; suivant : 001179Motifs involved in protein-protein interactions
Auteurs : C. Slingsby ; O. A. Bateman ; A. SimpsonSource :
- 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
Links to Exploration step
ISTEX:EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title 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><mods:affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</mods:affiliation></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><mods:affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</mods:affiliation></affiliation></author><author><name sortKey="Simpson, A" sort="Simpson, A" uniqKey="Simpson A" first="A." last="Simpson">A. Simpson</name><affiliation><mods:affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</mods:affiliation></affiliation></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></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><mods:affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</mods:affiliation></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><mods:affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</mods:affiliation></affiliation></author><author><name sortKey="Simpson, A" sort="Simpson, A" uniqKey="Simpson A" first="A." last="Simpson">A. Simpson</name><affiliation><mods:affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</mods:affiliation></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><istex><corpusName>springer-journals</corpusName><keywords><teeft><json:string>subunit</json:string><json:string>helix</json:string><json:string>immunoglobulin</json:string><json:string>dimer</json:string><json:string>biol</json:string><json:string>receptor</json:string><json:string>oligomer</json:string><json:string>constant domains</json:string><json:string>topology</json:string><json:string>polypeptide</json:string><json:string>variable domains</json:string><json:string>domain</json:string><json:string>edge strands</json:string><json:string>interface</json:string><json:string>monomer</json:string><json:string>identical subunits</json:string><json:string>helix bundles</json:string><json:string>barrel axes</json:string><json:string>helix bundle</json:string><json:string>protein domains</json:string><json:string>protein structure</json:string><json:string>amino acids</json:string><json:string>loop regions</json:string><json:string>intermolecular contacts</json:string><json:string>hydrophobic side chains</json:string><json:string>interface interactions</json:string><json:string>protein structures</json:string><json:string>dimer interface</json:string><json:string>first helix</json:string><json:string>cubic symmetry</json:string><json:string>long loop</json:string><json:string>long axes</json:string><json:string>extracellular domain</json:string><json:string>rotation axis</json:string><json:string>symmetrical assemblies</json:string><json:string>antiparallel strands</json:string><json:string>twofold axis</json:string><json:string>trends biochem</json:string><json:string>crystal structure</json:string><json:string>human growth hormone</json:string><json:string>linker region</json:string><json:string>tandem domains</json:string><json:string>human growth hormone receptor</json:string><json:string>different orientation</json:string><json:string>dimer formation</json:string><json:string>pseudo axis</json:string><json:string>sandwich structure</json:string><json:string>different subunits</json:string><json:string>dihydrolipoyl transacetylase</json:string><json:string>catalytic domain</json:string><json:string>dimer axis</json:string><json:string>strand</json:string></teeft></keywords><author><json:item><name>C. Slingsby</name><affiliations><json:string>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</json:string></affiliations></json:item><json:item><name>O. A. Bateman</name><affiliations><json:string>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</json:string></affiliations></json:item><json:item><name>A. Simpson</name><affiliations><json:string>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>motif</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>domain</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>interface</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>oligomer</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>helix-bundle</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>β-sheet</value></json:item></subject><articleId><json:string>BF00986727</json:string><json:string>Art4</json:string></articleId><arkIstex>ark:/67375/1BB-7H7030FS-6</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><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.</abstract><qualityIndicators><refBibsNative>false</refBibsNative><abstractWordCount>72</abstractWordCount><abstractCharCount>552</abstractCharCount><keywordCount>6</keywordCount><score>7.279</score><pdfWordCount>4415</pdfWordCount><pdfCharCount>27281</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>548 x 735 pts</pdfPageSize></qualityIndicators><title>Motifs involved in protein-protein interactions</title><pmid><json:string>8326954</json:string></pmid><genre><json:string>research-article</json:string></genre><host><title>Molecular Biology Reports</title><language><json:string>unknown</json:string></language><publicationDate>1993</publicationDate><copyrightDate>1993</copyrightDate><issn><json:string>0301-4851</json:string></issn><eissn><json:string>1573-4978</json:string></eissn><journalId><json:string>11033</json:string></journalId><volume>17</volume><issue>3</issue><pages><first>185</first><last>195</last></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Animal Biochemistry</value></json:item><json:item><value>Animal Anatomy / Morphology / Histology</value></json:item></subject></host><namedEntities><unitex><date></date><geogName></geogName><orgName></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName></persName><placeName></placeName><ref_url></ref_url><ref_bibl></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/1BB-7H7030FS-6</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Genetics</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - General Medicine</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1993</publicationDate><copyrightDate>1993</copyrightDate><doi><json:string>10.1007/BF00986727</json:string></doi><id>EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-7H7030FS-6/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-7H7030FS-6/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/1BB-7H7030FS-6/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Motifs involved in protein-protein interactions</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><availability><licence><p>Kluwer Academic Publishers, 1993</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</p></availability><date>1992-10-26</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>Special Issue: Protein-Protein Interactions</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Motifs involved in protein-protein interactions</title><author xml:id="author-0000"><persName><forename type="first">C.</forename><surname>Slingsby</surname></persName><affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</affiliation></author><author xml:id="author-0001"><persName><forename type="first">O.</forename><surname>Bateman</surname></persName><affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</affiliation></author><author xml:id="author-0002"><persName><forename type="first">A.</forename><surname>Simpson</surname></persName><affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</affiliation></author><idno type="istex">EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7</idno><idno type="ark">ark:/67375/1BB-7H7030FS-6</idno><idno type="DOI">10.1007/BF00986727</idno><idno type="article-id">BF00986727</idno><idno type="article-id">Art4</idno></analytic><monogr><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="pISSN">0301-4851</idno><idno type="eISSN">1573-4978</idno><idno type="journal-ID">true</idno><idno type="issue-article-count">5</idno><idno type="volume-issue-count">3</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="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></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1992-10-26</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Key words</head><item><term>motif</term></item><item><term>domain</term></item><item><term>interface</term></item><item><term>oligomer</term></item><item><term>helix-bundle</term></item><item><term>β-sheet</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Animal Biochemistry</term></item><item><term>Animal Anatomy / Morphology / Histology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1992-10-26">Created</change><change when="1993-04-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-7H7030FS-6/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//Springer-Verlag//DTD A++ V2.4//EN" URI="http://devel.springer.de/A++/V2.4/DTD/A++V2.4.dtd" name="istex:docType"></istex:docType><istex:document><Publisher><PublisherInfo><PublisherName>Kluwer Academic Publishers</PublisherName><PublisherLocation>Dordrecht</PublisherLocation></PublisherInfo><Journal><JournalInfo JournalProductType="ArchiveJournal" NumberingStyle="Unnumbered"><JournalID>11033</JournalID><JournalPrintISSN>0301-4851</JournalPrintISSN><JournalElectronicISSN>1573-4978</JournalElectronicISSN><JournalTitle>Molecular Biology Reports</JournalTitle><JournalSubTitle>An International Journal on Molecular and Cellular Biology</JournalSubTitle><JournalAbbreviatedTitle>Mol Biol Rep</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Life Sciences</JournalSubject><JournalSubject Type="Secondary">Animal Biochemistry</JournalSubject><JournalSubject Type="Secondary">Animal Anatomy / Morphology / Histology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>17</VolumeIDStart><VolumeIDEnd>17</VolumeIDEnd><VolumeIssueCount>3</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>3</IssueIDStart><IssueIDEnd>3</IssueIDEnd><IssueArticleCount>5</IssueArticleCount><IssueHistory><CoverDate><Year>1993</Year><Month>4</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>1993</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art4"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF00986727</ArticleID><ArticleDOI>10.1007/BF00986727</ArticleDOI><ArticleSequenceNumber>4</ArticleSequenceNumber><ArticleTitle Language="En">Motifs involved in protein-protein interactions</ArticleTitle><ArticleCategory>Special Issue: Protein-Protein Interactions</ArticleCategory><ArticleFirstPage>185</ArticleFirstPage><ArticleLastPage>195</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2004</Year><Month>12</Month><Day>30</Day></RegistrationDate><Received><Year>1992</Year><Month>10</Month><Day>26</Day></Received><Accepted><Year>1992</Year><Month>11</Month><Day>3</Day></Accepted></ArticleHistory><ArticleCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>1993</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>11033</JournalID><VolumeIDStart>17</VolumeIDStart><VolumeIDEnd>17</VolumeIDEnd><IssueIDStart>3</IssueIDStart><IssueIDEnd>3</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>C.</GivenName><FamilyName>Slingsby</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>O.</GivenName><GivenName>A.</GivenName><FamilyName>Bateman</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>A.</GivenName><FamilyName>Simpson</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Laboratory of Molecular Biology, Department of Crystallography</OrgDivision><OrgName>Birkbeck College</OrgName><OrgAddress><Street>Malet Street</Street><Postcode>WCIE 7HX</Postcode><City>London</City><Country>UK</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>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.</Para></Abstract><KeywordGroup Language="En"><Heading>Key words</Heading><Keyword>motif</Keyword><Keyword>domain</Keyword><Keyword>interface</Keyword><Keyword>oligomer</Keyword><Keyword>helix-bundle</Keyword><Keyword>β-sheet</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Motifs involved in protein-protein interactions</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Motifs involved in protein-protein interactions</title></titleInfo><name type="personal"><namePart type="given">C.</namePart><namePart type="family">Slingsby</namePart><affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">O.</namePart><namePart type="given">A.</namePart><namePart type="family">Bateman</namePart><affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Simpson</namePart><affiliation>Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, WCIE 7HX, London, UK</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateCreated encoding="w3cdtf">1992-10-26</dateCreated><dateIssued encoding="w3cdtf">1993-04-01</dateIssued><copyrightDate encoding="w3cdtf">1993</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract 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.</abstract><note>Special Issue: Protein-Protein Interactions</note><subject lang="en"><genre>Key words</genre><topic>motif</topic><topic>domain</topic><topic>interface</topic><topic>oligomer</topic><topic>helix-bundle</topic><topic>β-sheet</topic></subject><relatedItem type="host"><titleInfo><title>Molecular Biology Reports</title><subTitle>An International Journal on Molecular and Cellular Biology</subTitle></titleInfo><titleInfo type="abbreviated"><title>Mol Biol Rep</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">1993-04-01</dateIssued><copyrightDate encoding="w3cdtf">1993</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Animal Biochemistry</topic><topic>Animal Anatomy / Morphology / Histology</topic></subject><identifier type="ISSN">0301-4851</identifier><identifier type="eISSN">1573-4978</identifier><identifier type="JournalID">11033</identifier><identifier type="IssueArticleCount">5</identifier><identifier type="VolumeIssueCount">3</identifier><part><date>1993</date><detail type="volume"><number>17</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="pages"><start>185</start><end>195</end></extent></part><recordInfo><recordOrigin>Kluwer Academic Publishers, 1993</recordOrigin></recordInfo></relatedItem><identifier type="istex">EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7</identifier><identifier type="ark">ark:/67375/1BB-7H7030FS-6</identifier><identifier type="DOI">10.1007/BF00986727</identifier><identifier type="ArticleID">BF00986727</identifier><identifier type="ArticleID">Art4</identifier><accessCondition type="use and reproduction" contentType="copyright">Kluwer Academic Publishers, 1993</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Kluwer Academic Publishers, 1993</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-7H7030FS-6/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001178 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 001178 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:EEED224A2C7B03424ECDD3A66475ECAF53EFB0F7
|texte= Motifs involved in protein-protein interactions
}}
| This area was generated with Dilib version V0.6.33. |  |