Comparative Study
doi: 10.1038/358646a0.
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
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- PMID: 1379696
- DOI: 10.1038/358646a0
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Comparative Study
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
Nature.
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Abstract
Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet in the structure is flanked by two alpha-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino-aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate.
Comment in
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Signal transduction. Fishing in Src-infested waters.Nature. 1992 Aug 20;358(6388):625-6. doi: 10.1038/358625a0. Nature. 1992. PMID: 1379695 No abstract available.
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