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Crystal structure of Rnd3/RhoE: functional implications

MPG-Autoren

Fiegen,  Dennis
Max Planck Institute of Molecular Physiology, Max Planck Society;

Blumenstein,  Lars
Max Planck Institute of Molecular Physiology, Max Planck Society;

Stege,  Patricia
Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98734

Vetter,  Ingrid R.
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98673

Ahmadian,  Mohammad Reza
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Zitation

Fiegen, D., Blumenstein, L., Stege, P., Vetter, I. R., & Ahmadian, M. R. (2002). Crystal structure of Rnd3/RhoE: functional implications. FEBS Letters, 525(1-3): 1, pp. 100-104. Retrieved from http://dx.doi.org/10.1016/S0014-5793(02)03094-6.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-0E26-5
Zusammenfassung
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.