1CKB
STRUCTURAL BASIS FOR THE SPECIFIC INTERACTION OF LYSINE-CONTAINING PROLINE-RICH PEPTIDES WITH THE N-TERMINAL SH3 DOMAIN OF C-CRK
Summary for 1CKB
Entry DOI | 10.2210/pdb1ckb/pdb |
Descriptor | C-CRK N-TERMINAL SH3 DOMAIN, SOS PEPTIDE (PRO-PRO-PRO-VAL-PRO-PRO-ARG-ARG-ARG-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) More |
Total number of polymer chains | 2 |
Total formula weight | 8046.03 |
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 Cited by 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: 7735837DOI: 10.1016/S0969-2126(01)00151-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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