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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'''STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES'''
'''STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES'''
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[[Category: Wittinghofer, A.]]
[[Category: Wittinghofer, A.]]
[[Category: Wolthuis, R M.F.]]
[[Category: Wolthuis, R M.F.]]
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[[Category: signal transduction protein]]
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[[Category: Signal transduction protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:38:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:29:54 2008''
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Revision as of 04:38, 3 May 2008

Template:STRUCTURE 1rlf

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 Page seeded by OCA on Sat May 3 07:38:29 2008

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