DC Field | Value | Language |
---|---|---|
dc.contributor.author | Woo, Jae-Sung | ko |
dc.contributor.author | Suh, Hye-Young | ko |
dc.contributor.author | Park, Sam-Yong | ko |
dc.contributor.author | Oh, Byung-Ha | ko |
dc.date.accessioned | 2013-03-07T06:45:13Z | - |
dc.date.available | 2013-03-07T06:45:13Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2006-12 | - |
dc.identifier.citation | MOLECULAR CELL, v.24, no.6, pp.967 - 976 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.uri | http://hdl.handle.net/10203/89624 | - |
dc.description.abstract | B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets. | - |
dc.language | English | - |
dc.publisher | CELL PRESS | - |
dc.subject | UBIQUITIN LIGASES | - |
dc.subject | SOCS-BOX | - |
dc.subject | INTERACTION MAP | - |
dc.subject | SPRY-DOMAIN | - |
dc.subject | CELL-CYCLE | - |
dc.subject | RESTRICTION | - |
dc.subject | DESTRUCTION | - |
dc.subject | SPECIFICITY | - |
dc.subject | APOPTOSIS | - |
dc.subject | PRIMATES | - |
dc.title | Structural basis for protein recognition by B30.2/SPRY domains | - |
dc.type | Article | - |
dc.identifier.wosid | 000243253200016 | - |
dc.identifier.scopusid | 2-s2.0-33845663050 | - |
dc.type.rims | ART | - |
dc.citation.volume | 24 | - |
dc.citation.issue | 6 | - |
dc.citation.beginningpage | 967 | - |
dc.citation.endingpage | 976 | - |
dc.citation.publicationname | MOLECULAR CELL | - |
dc.identifier.doi | 10.1016/j.molcel.2006.11.009 | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.contributor.nonIdAuthor | Woo, Jae-Sung | - |
dc.contributor.nonIdAuthor | Suh, Hye-Young | - |
dc.contributor.nonIdAuthor | Park, Sam-Yong | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | SIGNALING | - |
dc.subject.keywordPlus | UBIQUITIN LIGASES | - |
dc.subject.keywordPlus | SOCS-BOX | - |
dc.subject.keywordPlus | INTERACTION MAP | - |
dc.subject.keywordPlus | SPRY-DOMAIN | - |
dc.subject.keywordPlus | CELL-CYCLE | - |
dc.subject.keywordPlus | RESTRICTION | - |
dc.subject.keywordPlus | DESTRUCTION | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | APOPTOSIS | - |
dc.subject.keywordPlus | PRIMATES | - |
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