未找到相关数据
CRYSTAL-STRUCTURE OF THE MAMMALIAN GRB2 ADAPTER
被引：194
作者：
MAIGNAN, S
GUILLOTEAU, JP
FROMAGE, N
ARNOUX, B
BECQUART, J
DUCRUIX, A
机构：
[1] UNIV PARIS SUD, STRUCT BIOL LAB, CNRS, UNITE MIXTE RECH, F-91198 GIF SUR YVETTE, FRANCE
[2] RHONE POULENC RORER, SERV BIOCHIM, F-94403 Vitry Sur Seine, FRANCE
来源：
关键词：
D O I：
10.1126/science.7716522
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：
The mammalian growth factor receptor- binding protein Grb2 is an adaptor that mediates activation of guanine nucleotide exchange on Ras. Grb2 binds to the receptor through its SH2 domain and to the carboxyl-terminal domain of Son of sevenless through its two SH3 domains. It is thus a key element in the signal transduction pathway. The crystal structure of Grb2 was determined to 3.1 angstrom resolution. The asymmetric unit is composed of an embedded dimer. The interlaced junctions between the SH2 and SH3 domains bring the two adjacent faces of the SH3 domains in van der Waals contact but leave room for the binding of proline-rich peptides.
引用
收藏
页码：291 / 293
页数：3
相关论文