2rgf | pdb_00002rgf

RBD OF RAL GUANOSINE-NUCLEOTIDE EXCHANGE FACTOR (PROTEIN), NMR, 10 STRUCTURES

spinqualitylabelsall models 2rgf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rgf is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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