2001
Crystal Structure of the Atypical Protein Kinase Domain of a TRP Channel with Phosphotransferase Activity
Yamaguchi H, Matsushita M, Nairn A, Kuriyan J. Crystal Structure of the Atypical Protein Kinase Domain of a TRP Channel with Phosphotransferase Activity. Molecular Cell 2001, 7: 1047-1057. PMID: 11389851, DOI: 10.1016/s1097-2765(01)00256-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCalcium ChannelsCrystallography, X-RayCyclic AMP-Dependent Protein KinasesEvolution, MolecularMiceModels, MolecularMolecular Sequence DataNucleotidesPhosphotransferasesProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentTRPC Cation ChannelsZincConceptsEukaryotic protein kinasesProtein kinaseTransient receptor potential channelsCatalytic domainKinase domainProtein kinase domainKinase catalytic domainDetectable sequence similarityATP-grasp domainEukaryotic cellsThreonine residuesSequence similarityChannel kinaseSequence comparisonCatalytic corePotential channelsMetabolic enzymesPhosphotransferase activityKinaseChannel functionTRP channelsExternal signalsUnexpected similaritiesWide distributionProtein
1998
Characterization of the Mechanism of Regulation of Ca2+/ Calmodulin-dependent Protein Kinase I by Calmodulin and by Ca2+/Calmodulin-dependent Protein Kinase Kinase*
Matsushita M, Nairn A. Characterization of the Mechanism of Regulation of Ca2+/ Calmodulin-dependent Protein Kinase I by Calmodulin and by Ca2+/Calmodulin-dependent Protein Kinase Kinase*. Journal Of Biological Chemistry 1998, 273: 21473-21481. PMID: 9705275, DOI: 10.1074/jbc.273.34.21473.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein Kinase KinaseCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCalmodulinCloning, MolecularEnzyme ActivationKineticsMolecular Sequence DataPhosphorylationProtein Serine-Threonine KinasesRatsConceptsProtein kinase IAbsence of CaMKinase ICalmodulin-dependent protein kinase IDetailed structure-function analysisDependent protein kinase IDependent protein kinase kinaseProtein kinase kinaseStructure-function analysisMechanism of regulationSpecific amino acidsEnzyme activityKinase kinaseAutoinhibited stateRegulatory domainCatalytic coreCaMKIMutant formsBasal enzyme activitySecond enzymeCaMKKAmino acidsAdditional mutationsMutationsActive form
1996
Structural Basis for the Autoinhibition of Calcium/Calmodulin-Dependent Protein Kinase I
Goldberg J, Nairn A, Kuriyan J. Structural Basis for the Autoinhibition of Calcium/Calmodulin-Dependent Protein Kinase I. Cell 1996, 84: 875-887. PMID: 8601311, DOI: 10.1016/s0092-8674(00)81066-1.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesCrystallographyImage Processing, Computer-AssistedMolecular Sequence DataPhosphorylationProtein ConformationProtein KinasesRatsSequence Homology, Amino AcidSubstrate SpecificityConceptsCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase IProtein kinase IKinase IRegulatory regionsATP-binding domainTerminal regulatory regionCatalytic domainCatalytic coreSecond helixStructural basisAlpha-helixCalmodulin targetsConformational changesPeptide substratesHelix segmentsCalmodulinHelixSubstantial structural changesRecognition elementInitial interactionInhibitory interactionsDomainAutoinhibitionCrystal structure