Equilibria between conformational states of the Ras oncogene protein revealed by high pressure crystallography.

ABSTRACT: In this work, we experimentally investigate the allosteric transitions between conformational states on the Ras oncogene protein using high pressure crystallography. Ras protein is a small GTPase involved in central regulatory processes occurring in multiple conformational states. Ras acts as a molecular switch between active GTP-bound, and inactive GDP-bound states, controlling essential signal transduction pathways. An allosteric network of interactions between the effector binding regions and the membrane interacting regions is involved in Ras cycling. The conformational states which coexist simultaneously in solution possess higher Gibbs free energy than the ground state. Equilibria between these states can be shifted by applying pressure favouring conformations with lower partial mola

SUBMITTER: Girard E 

PROVIDER: S-EPMC8848853 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature