Computational studies of the farnesyltransferase ternary complex part II: the conformational activation of farnesyldiphosphate.

ABSTRACT: Studies aimed at elucidating the reaction mechanism of farnesyltransferase (FTase), which catalyzes the prenylation of many cellular signaling proteins including Ras, has been an active area of research. Much is known regarding substrate binding and the impact of various catalytic site residues on catalysis. However, the molecular level details regarding the conformational rearrangement of farnesyldiphosphate (FPP), which has been proposed via structural analysis and mutagenesis studies to occur prior to the chemical step, is still poorly understood. Following on our previous computational characterization of the resting state of the FTase ternary complex, the thermodynamics of the conformational rearrangement step in the absence of magnesium was investigated for the wild type FTase and th

SUBMITTER: Cui G 

PROVIDER: S-EPMC2570014 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature