1SPR

BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS

Summary for 1SPR

• Entry DOI: 10.2210/pdb1spr/pdb
• Descriptor: SRC TYROSINE KINASE SH2 DOMAIN, PHOSPHATE ION (3 entities in total)
• Functional Keywords: transferase(phosphotransferase)
• Biological source: Rous sarcoma virus
• Total number of polymer chains: 4
• Total formula weight: 47976.89

Authors

Waksman, G.,Kuriyan, J. (deposition date: 1993-03-05, release date: 1994-05-31, Last modification date: 2024-02-14)

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

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: 7680960
DOI: 10.1016/0092-8674(93)90405-F

Experimental method

X-RAY DIFFRACTION (2.5 Å)