1sps
BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS
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OverviewOverview
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.
About this StructureAbout this Structure
1SPS is a Protein complex structure of sequences from Hamster polyomavirus and Rous sarcoma virus with PO3 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms., Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J, Cell. 1993 Mar 12;72(5):779-90. PMID:7680960
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