Structural highlights
Function
RND3_HUMAN Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of Rnd3/RhoE: functional implications.,Fiegen D, Blumenstein L, Stege P, Vetter IR, Ahmadian MR FEBS Lett. 2002 Aug 14;525(1-3):100-4. PMID:12163169[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. PMID:12163169
