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  Crystal structure of Rnd3/RhoE: functional implications

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.

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Genre: Journal Article
Alternative Title : FEBS Lett.

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 Creators:
Fiegen, Dennis1, Author
Blumenstein, Lars1, Author
Stege, Patricia1, Author
Vetter, Ingrid R.2, Author           
Ahmadian, Mohammad Reza3, Author           
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              
3Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753294              

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Free keywords: Rnd3; RhoE; RhoA; crystal structure; GTPase
 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 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.

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Language(s): eng - English
 Dates: 2002-08-14
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 6096
URI: http://dx.doi.org/10.1016/S0014-5793(02)03094-6
 Degree: -

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Title: FEBS Letters
  Alternative Title : FEBS Lett.
Source Genre: Journal
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Pages: - Volume / Issue: 525 (1-3) Sequence Number: 1 Start / End Page: 100 - 104 Identifier: -