pubmed-article:17189197 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:17189197 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:17189197 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:17189197 | pubmed:dateCreated | 2006-12-25 | lld:pubmed |
pubmed-article:17189197 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17189197 | pubmed:abstractText | 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. | lld:pubmed |
pubmed-article:17189197 | pubmed:language | eng | lld:pubmed |
pubmed-article:17189197 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17189197 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17189197 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17189197 | pubmed:month | Dec | lld:pubmed |
pubmed-article:17189197 | pubmed:issn | 1097-2765 | lld:pubmed |
pubmed-article:17189197 | pubmed:author | pubmed-author:OhByung-HaBH | lld:pubmed |
pubmed-article:17189197 | pubmed:author | pubmed-author:ParkSam-YongS... | lld:pubmed |
pubmed-article:17189197 | pubmed:author | pubmed-author:WooJae-SungJS | lld:pubmed |
pubmed-article:17189197 | pubmed:author | pubmed-author:SuhHye-YoungH... | lld:pubmed |
pubmed-article:17189197 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17189197 | pubmed:day | 28 | lld:pubmed |
pubmed-article:17189197 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:17189197 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17189197 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17189197 | pubmed:pagination | 967-76 | lld:pubmed |
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pubmed-article:17189197 | pubmed:meshHeading | pubmed-meshheading:17189197... | lld:pubmed |
pubmed-article:17189197 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:17189197 | pubmed:articleTitle | Structural basis for protein recognition by B30.2/SPRY domains. | lld:pubmed |
pubmed-article:17189197 | pubmed:affiliation | Center for Biomolecular Recognition, Department of Life Sciences, Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, Kyungbuk, 790-784, Korea. | lld:pubmed |
pubmed-article:17189197 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17189197 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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