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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), 100-104. doi:10.1016/S0014-5793(02)03094-6.

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FEBSLett_525_2002_100.pdf (Any fulltext), 376KB
 
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 Creators:
Fiegen, Dennis, Author
Blumenstein, Lars1, Author           
Stege, Patricia, Author
Vetter, Ingrid R., Author
Ahmadian, Mohammad Reza, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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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 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.

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Language(s): eng - English
 Dates: 2002-07-032002-04-302002-07-092002-07-202002-08-14
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 525 (1) Sequence Number: - Start / End Page: 100 - 104 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501