CRYSTAL-STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES

被引：642

作者：

WAKSMAN, G

KOMINOS, D

ROBERTSON, SC

PANT, N

BALTIMORE, D

BIRGE, RB

COWBURN, D

HANAFUSA, H

MAYER, BJ

OVERDUIN, M

RESH, MD

RIOS, CB

SILVERMAN, L

KURIYAN, J

机构：

[1] ROCKEFELLER UNIV, 1230 YORK AVE, NEW YORK, NY 10021 USA

[2] HOWARD HUGHES MED INST, NEW YORK, NY 10021 USA

[3] SLOAN KETTERING MEM CANC CTR, DEPT CELL BIOL & GENET, NEW YORK, NY 10021 USA

来源：

NATURE | 1992年 / 358卷 / 6388期

关键词：

D O I：

10.1038/358646a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 angstrom, 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.

引用

页码：646 / 653

页数：8

共 59 条

[1] BINDING OF SH2 DOMAINS OF PHOSPHOLIPASE-C-GAMMA-1, GAP, AND SRC TO ACTIVATED GROWTH-FACTOR RECEPTORS [J].