A Conserved Allosteric Pathway in Tyrosine Kinase Regulation
Marsiglia WM, Katigbak J, Zheng S, Mohammadi M, Zhang Y, Traaseth NJ. A Conserved Allosteric Pathway in Tyrosine Kinase Regulation. Structure 2019, 27: 1308-1315.e3. PMID: 31204250, PMCID: PMC6687525, DOI: 10.1016/j.str.2019.05.002.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationCatalytic DomainHumansHydrophobic and Hydrophilic InteractionsIsoleucineMagnetic Resonance SpectroscopyMolecular Dynamics SimulationMutationProtein ConformationProtein-Tyrosine KinasesConceptsTyrosine kinaseTyrosine kinase regulationAllosteric control mechanismReceptor tyrosine kinasesTyrosine kinase familyKinase regulationDFG motifActivation loopAllosteric pathwayKinase familyMutational disruptionKinase hingeInactive conformationHydrophobic residuesHuman diseasesKinaseConformational perturbationsCombination of NMREnzyme thermostabilityMutationsSkeletal syndromeActive siteMolecular dynamics simulationsThermostabilityStructural analysis