1ef5
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(New page: 200px<br /><applet load="1ef5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ef5" /> '''SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN...)
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Revision as of 11:50, 20 November 2007
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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
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