Adapter molecule crk

From Proteopedia

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spinqualitylabelsall models Structure of mouse Crk N terminal SH3 domain (magenta) complex with proline-rich peptide (green) (PDB entry 1cka) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Adapter 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 highlights Crk domains include several N-terminal SH2 and C-terminal SH3 domains. (1cka)[2] is shown.

3D structures of adpter molecule crk

Updated on 23-April-2018

1m30, 1m3a, 1m3b, 1m3c – mCrk N terminal SH3 (mutant) – mouse - NMR
2ggr – mCrk C terminal SH3 - NMR
2l3p, 2l3q, 2l3s – Crk residues 220-297 – chicken – NMR
1cka, 1ckb, 5ih2 – mCrk N terminal SH3 + proline-rich peptide
5l23 – mCrk N terminal SH3 + proline-rich peptide - NMR
1b07 – mCrk N terminal SH3 + SH3 peptoid inhibitor
5jn0 – hCrk SH2 - human
1ju5 – hCrk SH2 + phosphopeptide + Abl SH3
5ul6 – hCrk residues 134-191 + influenza virus proline-rich motif

References

1. ↑ 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
2. ↑ 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