1ef5

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[[Image:1ef5.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ef5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ef5 OCA], [http://www.ebi.ac.uk/pdbsum/1ef5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ef5 RCSB]</span>
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'''SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL'''
'''SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL'''
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[[Category: Shirouzu, M.]]
[[Category: Shirouzu, M.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: ra]]
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[[Category: Ra]]
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[[Category: ra]]
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[[Category: Ra]]
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[[Category: ras-binding domain]]
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[[Category: Ras-binding domain]]
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[[Category: rbd]]
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[[Category: Rbd]]
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[[Category: rgl]]
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[[Category: Rgl]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: Rsgi]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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Revision as of 12:01, 2 May 2008

Template:STRUCTURE 1ef5

SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL


Overview

The RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identified as a downstream effector of Ras. In the present study, the solution structure of the Ras-binding domain of RGL (RGL-RBD) was determined by NMR spectroscopy. The overall fold of RGL-RBD consists of a five-stranded beta-sheet and two alpha-helices, which is the same topology as that of RalGDS-RBD. The backbone chemical shift perturbation of RGL-RBD upon interaction with the GTP analog-bound Ras was also examined. The solution structure of RGL-RBD, especially around some of the Ras-interacting residues, is appreciably different from that of RalGDS-RBD.

About this Structure

1EF5 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Solution structure of the Ras-binding domain of RGL., Kigawa T, Endo M, Ito Y, Shirouzu M, Kikuchi A, Yokoyama S, FEBS Lett. 1998 Dec 28;441(3):413-8. PMID:9891982 Page seeded by OCA on Fri May 2 15:01:21 2008

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