G proteins, effectors and GAPs: structure and mechanism

被引：121

作者：

Sprang, SR

机构：

[1] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75235 USA

[2] Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75235 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1997年 / 7卷 / 06期

关键词：

D O I：

10.1016/S0959-440X(97)80157-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

G proteins form a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effecters. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein. (C) Current Biology Ltd ISSN 0959-440X.

引用

收藏

页码：849 / 856

页数：8

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