1rlf

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rlf OCA], [http://www.ebi.ac.uk/pdbsum/1rlf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rlf RCSB]</span>
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[[Category: signal transduction protein]]
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Revision as of 20:29, 30 March 2008


PDB ID 1rlf

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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