The Ras G Domain Lacks the Intrinsic Propensity to Form Dimers.

ABSTRACT: Ras GTPase is a molecular switch controlling a number of cellular pathways including growth, proliferation, differentiation, and apoptosis. Recent reports indicated that Ras undergoes dimerization at the membrane surface through protein-protein interactions. If firmly established this property of Ras would require profound reassessment of a large amount of published data and modification of the Ras signaling paradigm. One proposed mechanism of dimerization involves formation of salt bridges between the two GTPase domains (G domains) leading to formation of a compact dimer as observed in Ras crystal structures. In this work, we interrogated the intrinsic ability of Ras to self-associate in solution by creating conditions of high local concentration through irreversibly tethering the two G d

SUBMITTER: Kovrigina EA 

PROVIDER: S-EPMC4564675 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature