2rgd
From Proteopedia
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Crystal structure of H-RasQ61L-GppNHp
Overview
Transformation efficiencies of Ras mutants at residue 61 range over three, orders of magnitude, but the in vitro GTPase activity decreases 10-fold, for all mutants. We show that Raf impairs the GTPase activity of RasQ61L, suggesting that the Ras/Raf complex differentially modulates, transformation. Our crystal structures show that, in transforming mutants, switch II takes part in a network of hydrophobic interactions burying the, nucleotide and precatalytic water molecule. Our results suggest that Y32, and a water molecule bridging it to the gamma-phosphate in the wild-type, structure play a role in GTP hydrolysis in lieu of the Arg finger in the, absence of GAP. The bridging water molecule is absent in the transforming, mutants, contributing to the burying of the nucleotide. We propose a, mechanism for intrinsic hydrolysis in Raf-bound Ras and elucidate, structural features in the Q61 mutants that correlate with their potency, to transform cells.
About this Structure
2RGD is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Transformation Efficiency of RasQ61 Mutants Linked to Structural Features of the Switch Regions in the Presence of Raf., Buhrman G, Wink G, Mattos C, Structure. 2007 Dec;15(12):1618-29. PMID:18073111
Page seeded by OCA on Wed Jan 23 11:24:21 2008
Categories: Homo sapiens | Single protein | Buhrman, G. | Mattos, C. | Wink, G. | CA | GNP | MG | Disease mutation | Golgi apparatus | Gtp-binding | Gtpase | Lipoprotein | Membrane | Methylation | Molecular switch protein | Nucleotide-binding | Oncogene | Oncoprotein | Palmitate | Prenylation | Proto-oncogene | Signaling protein
