THE 2.2-ANGSTROM CRYSTAL-STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP-GAMMA-S

被引：715
作者：
NOEL, JP
HAMM, HE
SIGLER, PB
机构：
[1] YALE UNIV, BOYER CTR MOLEC MED, DEPT MOLEC BIOPHYS & BIOCHEM, 295 CONGRESS AVE, NEW HAVEN, CT 06510 USA
[2] YALE UNIV, BOYER CTR MOLEC MED, HOWARD HUGHES MED INST, NEW HAVEN, CT 06510 USA
[3] UNIV ILLINOIS, DEPT PHYSIOL & BIOPHYS, CHICAGO, IL 60680 USA
[4] UNIV SASSARI, IST FISIOL GEN & CHIM BIOL, I-07100 SASSARI, ITALY
来源：
NATURE | 1993年 / 366卷 / 6456期
关键词：
D O I：
10.1038/366654a0
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 2.2 angstrom crystal structure of activated rod transducin, G(talpha) . GTPgammaS, shows the bound GTPgammaS molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data.
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页码：654 / 663
页数：10
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