Adapter molecule crk: Difference between revisions
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== Function == | == Function == | ||
'''Adapter molecule crk''' (Crk) ('''C'''T10 '''R'''egulatior of '''K'''inase) or '''p38''' is a proto-oncogene which participates in the Reelin signaling cascade. Crk binds to several tyrosine-phosphorylated proteins.<ref>PMID:12086608</ref> | '''Adapter molecule crk''' (Crk) ('''C'''T10 '''R'''egulatior of '''K'''inase) or '''p38''' is a proto-oncogene which participates in the Reelin signaling cascade. Crk binds to several tyrosine-phosphorylated proteins.<ref>PMID:12086608</ref> See also [[SRC]] and [[Oncogenes & Tumor Suppressor Genes]]. | ||
== Structural highlights == | == Structural highlights == | ||
Latest revision as of 18:38, 20 January 2020
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] See also SRC and Oncogenes & Tumor Suppressor Genes. 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