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