Adapter molecule crk: Difference between revisions
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Crk domains include several N-terminal SH2 and C-terminal SH3 domains. <scene name='57/573988/Cv/4'>Mouse Crk N terminal SH3 domain complex with proline-rich peptide</scene> ([[1cka]])<ref>PMID:7735837</ref> is shown. | Crk domains include several N-terminal SH2 and C-terminal SH3 domains. <scene name='57/573988/Cv/4'>Mouse Crk N terminal SH3 domain complex with proline-rich peptide</scene> ([[1cka]])<ref>PMID:7735837</ref> is shown. | ||
==3D structures of | ==3D structures of adapter molecule crk== | ||
[[ | [[Adapter molecule crk 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
Revision as of 12:36, 21 March 2019
FunctionAdapter molecule crk (Crk) (CT10 Regulatior of Kinase) or p38 is a proto-oncogene which participates in the Reelin signaling cascade. Crk binds to several tyrosine-phosphorylated proteins.[1] Structural highlightsCrk domains include several N-terminal SH2 and C-terminal SH3 domains. (1cka)[2] is shown. 3D structures of adapter molecule crkAdapter molecule crk 3D structures
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ReferencesReferences
- ↑ Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. Molecular architecture and functional model of the endocytic AP2 complex. Cell. 2002 May 17;109(4):523-35. PMID:12086608
- ↑ Wu X, Knudsen B, Feller SM, Zheng J, Sali A, Cowburn D, Hanafusa H, Kuriyan J. Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure. 1995 Feb 15;3(2):215-26. PMID:7735837