GTPase-activating proteins: helping hands to complement an active site

被引：344

作者：

Scheffzek, K ^{[1
]}

Ahmadian, MR ^{[1
]}

Wittinghofer, A ^{[1
]}

机构：

[1] Max Planck Inst Mol Physiol, D-44139 Dortmund, Germany

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1998年 / 23卷 / 07期

关键词：

D O I：

10.1016/S0968-0004(98)01224-9

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：

Stimulation of the intrinsic GTPase activity of GTP-binding proteins by GTPase-activating proteins (GAPs) is a basic principle of GTP-binding-protein downregulation. Recently, the molecular mechanism behind this reaction has been elucidated by studies on Ras and Rho, and their respective GAPs. The basic features involve stabilizing the existing catalytic machinery and supplementing it by an external arginine residue. This represents a novel mechanism for enzyme active-site formation.

引用

页码：257 / 262

页数：6

共 57 条

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