G. Waksman, D. Kominos, S. Robertson, N. Pant, D. Baltimore, R.Birge, D. Cowburn, H. Hanafusa, B. Mayer, M. Overduin, M. Resh, C. Rios, L. Silverman and J. Kuriyan.
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides.
Nature. 358:646-653. (1992)

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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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