Crystal structure of Rnd3/RhoE: functional implications.

Article Details

Citation

Fiegen D, Blumenstein L, Stege P, Vetter IR, Ahmadian MR

Crystal structure of Rnd3/RhoE: functional implications.

FEBS Lett. 2002 Aug 14;525(1-3):100-4.

PubMed ID
12163169 [ View in PubMed
]
Abstract

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 A 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Rho-related GTP-binding protein RhoEP61587Details