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