1SPS
BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS
Summary for 1SPS
| Entry DOI | 10.2210/pdb1sps/pdb |
| Descriptor | SRC SH2 DOMAIN, PEPTIDE YEEI (3 entities in total) |
| Functional Keywords | transferase(phosphotransferase) |
| Biological source | Rous sarcoma virus More |
| Cellular location | Host membrane; Single-pass membrane protein (Potential): P03079 |
| Total number of polymer chains | 6 |
| Total formula weight | 40331.99 |
| Authors | Waksman, G.,Kuriyan, J. (deposition date: 1993-03-05, release date: 1994-05-31, Last modification date: 2024-10-30) |
| Primary citation | Waksman, G.,Shoelson, S.E.,Pant, N.,Cowburn, D.,Kuriyan, J. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell(Cambridge,Mass.), 72:779-790, 1993 Cited by PubMed Abstract: The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide has been determined at 2.7 A resolution by X-ray diffraction. The peptide binds in an extended conformation and makes primary interactions with the SH2 domain at six central residues: PQ(pY)EEI. The phosphotyrosine and the isoleucine are tightly bound by two well-defined pockets on the protein surface, resulting in a complex that resembles a two-pronged plug engaging a two-holed socket. The glutamate residues are in solvent-exposed environments in the vicinity of basic side chains of the SH2 domain, and the two N-terminal residues cap the phosphotyrosine-binding site. The crystal structure of Src SH2 in the absence of peptide has been determined at 2.5 A resolution, and comparison with the structure of the high affinity complex reveals only localized and relatively small changes. PubMed: 7680960DOI: 10.1016/0092-8674(93)90405-F PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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