Ontology highlight
ABSTRACT:
SUBMITTER: Aramini JM
PROVIDER: S-EPMC4963008 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Structure (London, England : 1993) 20150709 8
RAS binding is a critical step in the activation of BRAF protein serine/threonine kinase and stimulation of the mitogen-activated protein kinase signaling pathway. Mutations in both RAS and BRAF are associated with many human cancers. Here, we report the solution nuclear magnetic resonance (NMR) and X-ray crystal structures of the RAS-binding domain (RBD) from human BRAF. We further studied the complex between BRAF RBD and the GppNHp bound form of HRAS in solution. Backbone, side-chain, and (19) ...[more]