Adapter molecule crk
From Proteopedia
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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 == | ||
| - | Crk domains include several N-terminal SH2 and C-terminal SH3 domains. <scene name='57/573988/Cv/ | + | 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> | |
| - | [[1m30]], [[1m3a]], [[1m3b]], [[1m3c]] – mCrk N terminal SH3 (mutant) – mouse - NMR<br /> | ||
| - | [[2ggr]] – mCrk C terminal SH3 - NMR<br /> | ||
| - | [[2l3p]], [[2l3q]], [[2l3s]] – Crk residues 220-297 – chicken – NMR<br /> | ||
| - | [[1cka]], [[1ckb]], [[5ih2]] – mCrk N terminal SH3 + proline-rich peptide<br /> | ||
| - | [[5l23]] – mCrk N terminal SH3 + proline-rich peptide - NMR<br /> | ||
| - | [[1b07]] – mCrk N terminal SH3 + SH3 peptoid inhibitor<br /> | ||
| - | [[5jn0]] – hCrk SH2 - human<br /> | ||
| - | [[1ju5]] – hCrk SH2 + phosphopeptide + Abl SH3 <br /> | ||
| - | [[5ul6]] – hCrk residues 134-191 + influenza virus proline-rich motif <br /> | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ 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
