| pubmed-article:17255936 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C0038250 | lld:lifeskim |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C0206364 | lld:lifeskim |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:17255936 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:17255936 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:17255936 | pubmed:dateCreated | 2007-2-8 | lld:pubmed |
| pubmed-article:17255936 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17255936 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17255936 | pubmed:abstractText | Stem cell factor (SCF) binds to and activates the KIT receptor, a class III receptor tyrosine kinase (RTK), to stimulate diverse processes including melanogenesis, gametogenesis and hematopoeisis. Dysregulation of KIT activation is associated with many cancers. We report a 2.5 A crystal structure of the functional core of SCF bound to the extracellular ligand-binding domains of KIT. The structure reveals a 'wrapping' SCF-recognition mode by KIT, in which KIT adopts a bent conformation to facilitate each of its first three immunoglobulin (Ig)-like domains to interact with SCF. Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding. The SCF/KIT complex reveals a unique RTK dimerization assembly, and a novel recognition mode between four-helix bundle cytokines and Ig-family receptors. It serves as a framework for understanding the activation mechanisms of class III RTKs. | lld:pubmed |
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| pubmed-article:17255936 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17255936 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17255936 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17255936 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17255936 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17255936 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17255936 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17255936 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:17255936 | pubmed:author | pubmed-author:ChenXiaoyanX | lld:pubmed |
| pubmed-article:17255936 | pubmed:author | pubmed-author:FociaPamela... | lld:pubmed |
| pubmed-article:17255936 | pubmed:author | pubmed-author:LiuHeliH | lld:pubmed |
| pubmed-article:17255936 | pubmed:author | pubmed-author:HeXiaolinX | lld:pubmed |
| pubmed-article:17255936 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17255936 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:17255936 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:17255936 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17255936 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17255936 | pubmed:pagination | 891-901 | lld:pubmed |
| pubmed-article:17255936 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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