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Comparative Study
. 1992 Aug 20;358(6388):646-53.
doi: 10.1038/358646a0.

Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

G Waksman  1 , D Kominos, S C Robertson, N Pant, D Baltimore, R B Birge, D Cowburn, H Hanafusa, B J Mayer, M Overduin, M D Resh, C B Rios, L Silverman, J Kuriyan
Affiliations
Comparative Study

Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

G Waksman et al. Nature. .

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.

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