Disruption of the EGFR E884–R958 ion pair conserved in the human kinome differentially alters signaling and inhibitor sensitivity
Tang Z, Jiang S, Du R, Petri E, El-Telbany A, Chan P, Kijima T, Dietrich S, Matsui K, Kobayashi M, Sasada S, Okamoto N, Suzuki H, Kawahara K, Iwasaki T, Nakagawa K, Kawase I, Christensen J, Hirashima T, Halmos B, Salgia R, Boggon T, Kern J, Ma P. Disruption of the EGFR E884–R958 ion pair conserved in the human kinome differentially alters signaling and inhibitor sensitivity. Oncogene 2008, 28: 518-533. PMID: 19015641, PMCID: PMC2633425, DOI: 10.1038/onc.2008.411.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAMP-Activated Protein Kinase KinasesAnimalsChlorocebus aethiopsCOS CellsErbB ReceptorsErlotinib HydrochlorideFocal Adhesion Kinase 1HumansIndolesLung NeoplasmsMAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mutation, MissensePiperazinesProtein ConformationProtein Kinase InhibitorsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-kitProto-Oncogene Proteins c-metProto-Oncogene Proteins c-retQuinazolinesReceptors, Growth FactorSulfonamidesConceptsHuman kinomeEpidermal growth factor receptorKinase substrate recognitionInhibitor sensitivityCancer-associated mutationsSystematic bioinformatics analysisTumor suppressor geneSmall molecule inhibitorsSubstrate recognitionProtein kinaseGrowth factor receptorBioinformatics analysisHomologous residuesDownstream signalingSequence analysisLysine residuesKinomeC-lobeConformational changesFamily inhibitorsMutation cataloguesAdjacent residuesMET inhibitor SU11274Factor receptorMutations