Data suggest that isoform-specific sequences in the allosteric lobes of HRAS KRAS and NRAS have an impact on biocatalysis (kinetics of GTP hydrolysis) and interaction with c-Raf kinase which must be due to allosteric effects on dynamics and conformational states given the identical active sites of these isoenzymes.
Results shows the structural characterization of NRAS isoform 5 which overexpression results in more aggressive phenotype of melanoma. The protein was found highly flexible in aqueous solution but forms a helix-turn-coil structure in the presence of trifluoroethanol.
The neutron crystal structure presented here puts in question our understanding of the pre-catalytic state associated with the hydrolysis reaction central to the function of RAS and other GTPases.
Backbone conformational flexibility of the lipid modified membrane anchor of the human N-Ras protein investigated by solid-state NMR and molecular dynamics simulation.
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