Ontology highlight
ABSTRACT:
SUBMITTER: Cookis T
PROVIDER: S-EPMC8301913 | biostudies-literature | 2021 Jul
REPOSITORIES: biostudies-literature
Cookis Trinity T Mattos Carla C
Biomolecules 20210707 7
Ras and Raf-kinase interact through the Ras-binding (RBD) and cysteine-rich domains (CRD) of Raf to signal through the mitogen-activated protein kinase pathway, yet the molecular mechanism leading to Raf activation has remained elusive. We present the 2.8 Å crystal structure of the HRas-CRaf-RBD_CRD complex showing the Ras-Raf interface as a continuous surface on Ras, as seen in the KRas-CRaf-RBD_CRD structure. In molecular dynamics simulations of a Ras dimer model formed through the α4-α5 inter ...[more]