Phosphorylation of RAF Kinase Dimers Drives Conformational Changes that Facilitate Transactivation
Jambrina P, Rauch N, Pilkington R, Rybakova K, Nguyen L, Kholodenko B, Buchete N, Kolch W, Rosta E. Phosphorylation of RAF Kinase Dimers Drives Conformational Changes that Facilitate Transactivation. Angewandte Chemie 2015, 128: 995-998. DOI: 10.1002/ange.201509272.Peer-Reviewed Original ResearchRAF dimerizationStructure-based mechanismPhysiological activation mechanismKinase dimerΑC-helixAcidic motifRaf kinaseRAF dimersR-spineConformational changesTrp residuesRAF inhibitorsPhosphorylationActivation mechanismKey playersSalt bridgeMotifKinaseCooperative interactionsRafPersonalized cancer therapyActive siteImportant targetResiduesPathway