1rlf
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(New page: 200px<br /><applet load="1rlf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rlf" /> '''STRUCTURE DETERMINATION OF THE RAS-BINDING D...)
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Revision as of 23:33, 20 November 2007
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STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES
Overview
Ral-specific guanine nucleotide exchange factors RalGDS, Rgl, and Rlf have, been suggested to function as intermediates between Ras and Ral pathways, by being able to bind Ras proteins through their C-terminal Ras-binding, domains (RBD). The RBDs of RalGDS and of the Ser/Thr kinase c-Raf-1 have, been shown to have the same tertiary structure. In contrast to the RBDs of, Raf and RalGDS, which bind either Ras or Rap with high affinity, Rlf-RBD, has a similar affinity for both GTP-binding proteins. To be able to, compare these RBDs on a structural level, we have solved the, three-dimensional structure of Rlf-RBD by NMR spectroscopy. The overall, tertiary structure of Rlf-RBD shows the, betabetaalphabetabetaalphabeta-fold of the ubiquitin superfamily and is, very similar to that of RalGDS-RBD. The binding interface of Rlf-RBD to, Ras was mapped using chemical shift analysis and indicated a binding mode, similar to that in the case of Rap.Raf-RBD. However, comparison of the, putatively interacting regions revealed structural differences which are, proposed to be responsible for the different substrate affinities of Rlf-, RalGDS-, and Raf-RBD.
About this Structure
1RLF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf., Esser D, Bauer B, Wolthuis RM, Wittinghofer A, Cool RH, Bayer P, Biochemistry. 1998 Sep 29;37(39):13453-62. PMID:9753431
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