Path Sampling Simulations Reveal How the Q61L Mutation Alters the Dynamics of KRas.

ABSTRACT: Flexibility is essential for many proteins to function, but can be difficult to characterize. Experiments lack resolution in space and time, while the time scales involved are prohibitively long for straightforward molecular dynamics simulations. In this work, we present a multiple state transition path sampling simulation study of a protein that has been notoriously difficult to characterize in its active state. The GTPase enzyme KRas is a signal transduction protein in pathways for cell differentiation, growth, and division. When active, KRas tightly binds guanosine triphosphate (GTP) in a rigid state. The protein-GTP complex can also visit more flexible states, in which it is not active. KRas mutations can affect the conversion between these rigid and flexible states, thus prolonging th

SUBMITTER: Roet S 

PROVIDER: S-EPMC9743084 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature