Structure of the TRPA1 ion channel suggests regulatory mechanisms
Paulsen CE, Armache JP, Gao Y, Cheng Y, Julius D. Structure of the TRPA1 ion channel suggests regulatory mechanisms. Nature 2015, 520: 511-517. PMID: 25855297, PMCID: PMC4409540, DOI: 10.1038/nature14367.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAnalgesicsAnkyrin RepeatAnti-Inflammatory AgentsBinding SitesCalcium ChannelsCryoelectron MicroscopyCytosolHumansModels, MolecularNerve Tissue ProteinsPolyphosphatesProtein StabilityProtein SubunitsStructure-Activity RelationshipTransient Receptor Potential ChannelsTRPA1 Cation ChannelConceptsTRPA1 ion channelsCoil assembly domainIon channelsCovalent protein modificationSingle-particle electronAnti-inflammatory agentsTransient receptor potentialStructure-based designAllosteric domainProtein modificationRegulatory mechanismsChannel regulationNoxious chemical agentsTRPA1 regulationAssembly domainIrritant exposureTRPA1 antagonistInflammatory conditionsTissue injuryTRPA1 functionStructural mechanismsDrug metabolismPotent antagonistReceptor potentialHuman TRPA1