1QWE
C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND APP12
Summary for 1QWE
| Entry DOI | 10.2210/pdb1qwe/pdb |
| Descriptor | TYROSINE-PROTEIN KINASE TRANSFORMING PROTEIN SRC, ALA-PRO-PRO-LEU-PRO-PRO-ARG-ASN-ARG-PRO-ARG-LEU (2 entities in total) |
| Functional Keywords | src sh3 domain, class ii ligand complex, complex (signal transduction-peptide) complex, complex (signal transduction/peptide) |
| Biological source | Avian sarcoma virus |
| Total number of polymer chains | 2 |
| Total formula weight | 8491.42 |
| Authors | Feng, S.,Chiyoshi, K.,Rickles, R.J.,Schreiber, S.L. (deposition date: 1995-11-09, release date: 1996-03-08, Last modification date: 2024-05-22) |
| Primary citation | Feng, S.,Kasahara, C.,Rickles, R.J.,Schreiber, S.L. Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc.Natl.Acad.Sci.USA, 92:12408-12415, 1995 Cited by PubMed Abstract: Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligant residues flanking the proline-rich core. The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity. PubMed: 8618911DOI: 10.1073/pnas.92.26.12408 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
