Crystal structure of Rnd3/RhoE: functional implications

被引：33

作者：

Fiegen, D ^{[1
]}

Blumenstein, L ^{[1
]}

Stege, P ^{[1
]}

Vetter, IR ^{[1
]}

Ahmadian, MR ^{[1
]}

机构：

[1] Max Planck Inst Mol Physiol, Abt Strukturelle Biol, D-44227 Dortmund, Germany

来源：

FEBS LETTERS | 2002年 / 525卷 / 1-3期

关键词：

Rnd3; RhoE; RhoA; crystal structure; GTPase;

D O I：

10.1016/S0014-5793(02)03094-6

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：

The Rnd proteins constitute an exceptional subfamily within the Rho GTPase family. They possess extended chains at both termini and four prominent amino acid deviations causing GTPase deficiency. Herein, we report the crystal structure of the Rnd3/RhoE G-domain (amino acids 19-200) at 2.0 Angstrom resolution. This is the first GTP-structure of a Rho family member which reveals a similar fold but striking differences from RhoA concerning (i) GTPase center, (ii) charge distribution at several surface areas, (iii) C3-transferase binding site and (iv) interacting interfaces towards RhoA regulators and effectors. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：100 / 104

页数：5

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