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Crystal structure of the rat REM2 GTPase - G domain bound to GDPCrystal structure of the rat REM2 GTPase - G domain bound to GDP
Structural highlights
FunctionREM2_RAT Binds GTP saturably and exhibits a low intrinsic rate of GTP hydrolysis. Publication Abstract from PubMedRGK proteins are atypical small GTP-binding proteins that are involved in the regulation of voltage-dependent calcium channels and actin cytoskeleton remodelling. The structure of the Rem2 G domain bound to GDP is reported here in a monoclinic crystal form at 2.66 A resolution. It is very similar to the structure determined previously from an orthorhombic crystal form. However, differences in the crystal-packing environment revealed that the switch I and switch II regions are flexible and not ordered as previously reported. Comparison of the available RGK protein structures along with those of other small GTP-binding proteins highlights two structural features characteristic of this atypical family and suggests that the conserved tryptophan residue in the DXWEX motif may be a structural determinant of the nucleotide-binding affinity. Structure of the GDP-bound G domain of the RGK protein Rem2.,Reymond P, Coquard A, Chenon M, Zeghouf M, El Marjou A, Thompson A, Menetrey J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):626-31., Epub 2012 May 22. PMID:22684057[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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