Structural highlights
Function
GNDS_HUMAN Stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. Interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The solution structure of the Ras-binding domain (RBD) of Ral guanine-nucleotide exchange factor RalGEF was solved by NMR spectroscopy. The overall structure is similar to that of Raf-RBD, another effector of Ras, although the sequence identity is only 13%. 15N chemical shifts changes in the complex of RalGEF-RBD with Ras indicate an interaction similar to the intermolecular beta-sheet observed for the complex between Ras and Raf-RBD.
Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling.,Geyer M, Herrmann C, Wohlgemuth S, Wittinghofer A, Kalbitzer HR Nat Struct Biol. 1997 Sep;4(9):694-9. PMID:9302994[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Geyer M, Herrmann C, Wohlgemuth S, Wittinghofer A, Kalbitzer HR. Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling. Nat Struct Biol. 1997 Sep;4(9):694-9. PMID:9302994
