Crystal structure of Rnd3/RhoE: functional implications 1

FEBS Letters

Blumenstein, Lars¹  Vetter, Ingrid R¹  Fiegen, Dennis¹  Ahmadian, Mohammad Reza¹  Stege, Patricia¹ 

[1] Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany

关键词: Rnd3;    RhoE;    RhoA;    Crystal structure;    GTPase;   

DOI  :  10.1016/S0014-5793(02)03094-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 Å 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.

【 授权许可】

Unknown