| pubmed-article:12551896 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C1366512 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:12551896 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:12551896 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:12551896 | pubmed:dateCreated | 2003-4-7 | lld:pubmed |
| pubmed-article:12551896 | pubmed:abstractText | Grb7, Grb10, and Grb14 are members of a distinct family of adapter proteins that interact with various receptor tyrosine kinases upon receptor activation. Proteins in this family contain several modular signaling domains including a pleckstrin homology (PH) domain, a BPS (between PH and SH2) domain, and a C-terminal Src homology 2 (SH2) domain. Although SH2 domains are typically monomeric, we show that the Grb10 SH2 domain and also full-length Grb10 gamma are dimeric in solution under physiologic conditions. The crystal structure of the Grb10 SH2 domain at 1.65-A resolution reveals a non-covalent dimer whose interface comprises residues within and flanking the C-terminal alpha helix, which are conserved in the Grb7/Grb10/Grb14 family but not in other SH2 domains. Val-522 in the BG loop (BG3) and Asp-500 in the EF loop (EF1) are positioned to interfere with the binding of the P+3 residue of a phosphopeptide ligand. These structural features of the Grb10 SH2 domain will favor binding of dimeric, turn-containing phosphotyrosine sequences, such as the phosphorylated activation loops in the two beta subunits of the insulin and insulin-like growth factor-1 receptors. Moreover, the structure suggests the mechanism by which the Grb7 SH2 domain binds selectively to pTyr-1139 (pYVNQ) in Her2, which along with Grb7 is co-amplified in human breast cancers. | lld:pubmed |
| pubmed-article:12551896 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12551896 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12551896 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12551896 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12551896 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12551896 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12551896 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12551896 | pubmed:author | pubmed-author:HubbardStevan... | lld:pubmed |
| pubmed-article:12551896 | pubmed:author | pubmed-author:GhirlandoRodo... | lld:pubmed |
| pubmed-article:12551896 | pubmed:author | pubmed-author:SteinEvan GEG | lld:pubmed |
| pubmed-article:12551896 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12551896 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:12551896 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12551896 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12551896 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12551896 | pubmed:pagination | 13257-64 | lld:pubmed |
| pubmed-article:12551896 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12551896 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12551896 | pubmed:articleTitle | Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificity. | lld:pubmed |
| pubmed-article:12551896 | pubmed:affiliation | Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA. | lld:pubmed |
| pubmed-article:12551896 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12551896 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12551896 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12551896 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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