spacer BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS
Primary citation
Title Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms.
Authors Waksman, G.search; Shoelson, S.E.search; Pant, N.search; Cowburn, D.search; Kuriyan, J.search
Journal CELL(CAMBRIDGE,MASS.)search vol:72, pag:779-790 (1993), Identifiers: PubMed ID (7680960)search DOI (10.1016/0092-8674(93)90405-F)
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.
MeSH terms Amino Acid Sequencesearch, Binding Sitessearch, Glutamatessearch, Glutamic Acidsearch, Modelssearch, Molecularsearch, Molecular Sequence Datasearch, Phosphopeptidessearch, Protein Conformationsearch, Proto-Oncogene Proteins pp60(c-src)search, Sequence Alignmentsearch, Tyrosinesearch, X-Ray Diffractionsearch
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