2005
Control of the CFTR channel's gates.
Vergani P, Basso C, Mense M, Nairn A, Gadsby D. Control of the CFTR channel's gates. Biochemical Society Transactions 2005, 33: 1003-7. PMID: 16246032, PMCID: PMC2728124, DOI: 10.1042/bst20051003.Peer-Reviewed Original ResearchConceptsChannel gateIon channelsProtein family membersNBD dimer interfaceAnion-selective poreEvolutionary conservationABC proteinsCFTR moleculesForm homodimersTransmembrane domainATP bindingHeterodimer interfaceDimer interfaceMolecular mechanismsTight dimerizationNBDATPSingle-channel recordingsResiduesFamily membersNBD1NBD2Cystic fibrosis patientsMutagenesisHomodimer
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
1999
Control of CFTR Channel Gating by Phosphorylation and Nucleotide Hydrolysis
GADSBY D, NAIRN A. Control of CFTR Channel Gating by Phosphorylation and Nucleotide Hydrolysis. Physiological Reviews 1999, 79: s77-s107. PMID: 9922377, DOI: 10.1152/physrev.1999.79.1.s77.Peer-Reviewed Original ResearchConceptsNucleotide-binding domainCFTR channelsCytoplasmic nucleotide-binding domainsNucleotide hydrolysisChannel gatingDependent phosphorylation eventsCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelCFTR channel currentsCFTR channel gatingATP moleculesLarge cytoplasmic domainCommon lethal genetic diseaseSecond ATP moleculeSingle CFTR channelsATP hydrolysis cycleLethal genetic diseasePhosphorylation eventsGating cycleRegulatory domainCytoplasmic domainDifferent phosphoformsProgressive phosphorylationMultiple proteinsProtein productsHydrolysis cycle
1977
The equilibrium constant and the reversibility of the reaction catalysed by nicotinamide-adenine dinucleotide kinase from pigeon liver
Apps D, Nairn A. The equilibrium constant and the reversibility of the reaction catalysed by nicotinamide-adenine dinucleotide kinase from pigeon liver. Biochemical Journal 1977, 167: 87-93. PMID: 201249, PMCID: PMC1183625, DOI: 10.1042/bj1670087.Peer-Reviewed Original Research