Adapter molecule crk

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.

Structure of mouse Crk N terminal SH3 domain (grey) complex with proline-rich peptide (green) (PDB entry 1cka)

Drag the structure with the mouse to rotate

3D structures of adpter molecule crk3D structures of adpter molecule crk

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 – mCrk N terminal SH3 + proline-rich peptide
1b07 – mCrk N terminal SH3 + SH3 peptoid inhibitor
1ju5 – hCrk SH2 + phosphopeptide + Abl SH3 - human

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[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

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