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 Ras-interacting domains of the the protein-kinase Raf and the Ral guanine nucleotide dissociation stimulator, RalGDS, lack extensive sequence similarity, but their overall three-dimensional structures are very similar to each other. Mutational analysis indicated that three residues in the RalGDS domain are critical for its interaction with Ras.
Three-dimensional structure of the Ras-interacting domain of RalGDS.,Huang L, Weng X, Hofer F, Martin GS, Kim SH Nat Struct Biol. 1997 Aug;4(8):609-15. PMID:9253406[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huang L, Weng X, Hofer F, Martin GS, Kim SH. Three-dimensional structure of the Ras-interacting domain of RalGDS. Nat Struct Biol. 1997 Aug;4(8):609-15. PMID:9253406
