Computational and biochemical characterization of two partially overlapping interfaces and multiple weak-affinity K-Ras dimers.

ABSTRACT: Recent studies found that membrane-bound K-Ras dimers are important for biological function. However, the structure and thermodynamic stability of these complexes remained unknown because they are hard to probe by conventional approaches. Combining data from a wide range of computational and experimental approaches, here we describe the structure, dynamics, energetics and mechanism of assembly of multiple K-Ras dimers. Utilizing a range of techniques for the detection of reactive surfaces, protein-protein docking and molecular simulations, we found that two largely polar and partially overlapping surfaces underlie the formation of multiple K-Ras dimers. For validation we used mutagenesis, electron microscopy and biochemical assays under non-denaturing conditions. We show that partial disru

SUBMITTER: Prakash P 

PROVIDER: S-EPMC5220301 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature