1RLF

STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES

Summary for 1RLF

• Entry DOI: 10.2210/pdb1rlf/pdb
• Descriptor: RLF (1 entity in total)
• Functional Keywords: signal transduction protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 10048.38

Authors

Esser, D.,Bauer, B.,Wolthuis, R.M.F.,Wittinghofer, A.,Cool, R.H.,Bay, P. (deposition date: 1998-07-09, release date: 1999-02-16, Last modification date: 2024-05-22)

Primary citation

Esser, D.,Bauer, B.,Wolthuis, R.M.,Wittinghofer, A.,Cool, R.H.,Bayer, P.
Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf.
Biochemistry, 37:13453-13462, 1998

PubMed Abstract: 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.

PubMed: 9753431
DOI: 10.1021/bi9811664

Experimental method

SOLUTION NMR