1CKA

STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK

Summary for 1CKA

• Entry DOI: 10.2210/pdb1cka/pdb
• Descriptor: C-CRK N-TERMINAL SH3 DOMAIN, C3G PEPTIDE (PRO-PRO-PRO-ALA-LEU-PRO-PRO-LYS-LYS-ARG) (3 entities in total)
• Functional Keywords: complex (oncogene protein-peptide), complex (oncogene protein-peptide) complex, complex (oncogene protein/peptide)
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 7917.92

Authors

Wu, X.,Kuriyan, J. (deposition date: 1995-01-24, release date: 1995-05-08, Last modification date: 2024-02-07)

Primary citation

Wu, X.,Knudsen, B.,Feller, S.M.,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, 3:215-226, 1995

PubMed Abstract: Proline-rich segments in the guanine nucleotide exchange factor C3G bind much more strongly to the N-terminal Src homology 3 domain (SH3-N) of the proto-oncogene product c-Crk than to other SH3 domains. The presence of a lysine instead of an arginine in the peptides derived from C3G appears to be crucial for this specificity towards c-Crk.

PubMed: 7735837
DOI: 10.1016/S0969-2126(01)00151-4

Experimental method

X-RAY DIFFRACTION (1.5 Å)