Modeling of RAS complexes supports roles in cancer for less studied partners.

ABSTRACT:

Background

RAS protein interactions have predominantly been studied in the context of the RAF and PI3kinase oncogenic pathways. Structural modeling and X-ray crystallography have demonstrated that RAS isoforms bind to canonical downstream effector proteins in these pathways using the highly conserved switch I and II regions. Other non-canonical RAS protein interactions have been experimentally identified, however it is not clear whether these proteins also interact with RAS via the switch regions.

Results

To address this question we constructed a RAS isoform-specific protein-protein interaction network and predicted 3D complexes involving RAS isoforms and interaction partners to identify the most probable interaction interfaces. The resulting models correctly captured the bi

SUBMITTER: Engin HB 

PROVIDER: S-EPMC5558186 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature