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The mechanism of Raf activation through dimerization

Mingzhen Zhang, Ryan Maloney, Hyunbum Jang, Ruth Nussinov

2021Chemical Science56 citationsDOIOpen Access PDF

Abstract

-autophosphorylation. Once fully activated, the ON-state kinase domain can be stabilized by a newly identified functional N-terminal basic (NtB) motif in the dimer for Raf signaling. This work provides atomic level insight into critical steps in Raf activation and outlines a new venue for drug discovery against Raf dimerization.

Topics & Concepts

AutophosphorylationDimerProtein kinase domainChemistryKinaseStackingPhosphorylationSerineCell biologyMAPK/ERK pathwaySignal transductionProtein kinase AEnzyme activatorStereochemistryBiochemistryBiophysicsBiologyMutantOrganic chemistryGeneMelanoma and MAPK PathwaysProtein Kinase Regulation and GTPase SignalingComputational Drug Discovery Methods
The mechanism of Raf activation through dimerization | Litcius