Structural analysis of the mechanism of phosphorylation of a critical autoregulatory tyrosine residue in FGFR1 kinase domain
Kobashigawa Y, Amano S, Yokogawa M, Kumeta H, Morioka H, Inouye M, Schlessinger J, Inagaki F. Structural analysis of the mechanism of phosphorylation of a critical autoregulatory tyrosine residue in FGFR1 kinase domain. Genes To Cells 2015, 20: 860-870. PMID: 26300540, DOI: 10.1111/gtc.12277.Peer-Reviewed Original ResearchConceptsFGFR1 kinase domainKinase domainFibroblast growth factor receptor 1Catalytic domainCovalent cross-linking experimentsReceptor tyrosine kinase activationNormal cellular processesSignal transduction pathwaysNonreceptor tyrosine kinaseMechanism of phosphorylationTyrosine kinase activationCross-linking experimentsInitial phosphorylation stepActivation loopCellular processesTransient dimer formationTransduction pathwaysTyrosine phosphorylationGrowth factor receptor 1Domain interactionsKinase activationMutational analysisContact sitesMolecular mechanismsTyrosine residues