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dc.creatorPalovcak, E
dc.creatorDelemotte, L
dc.creatorKlein, ML
dc.creatorCarnevale, V
dc.date.accessioned2021-01-31T16:20:01Z
dc.date.available2021-01-31T16:20:01Z
dc.date.issued2015-01-01
dc.identifier.issn0022-1295
dc.identifier.issn1540-7748
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/5252
dc.identifier.other26078053 (pubmed)
dc.identifier.urihttp://hdl.handle.net/20.500.12613/5270
dc.description.abstract© 2015 Palovcak et al. The transient receptor potential (TRP) channel superfamily plays a central role in transducing diverse sensory stimuli in eukaryotes. Although dissimilar in sequence and domain organization, all known TRP channels act as polymodal cellular sensors and form tetrameric assemblies similar to those of their distant relatives, the voltagegated potassium (Kv) channels. Here, we investigated the related questions of whether the allosteric mechanism underlying polymodal gating is common to all TRP channels, and how this mechanism differs from that underpinning Kv channel voltage sensitivity. To provide insight into these questions, we performed comparative sequence analysis on large, comprehensive ensembles of TRP and Kv channel sequences, contextualizing the patterns of conservation and correlation observed in the TRP channel sequences in light of the well-studied Kv channels. We report sequence features that are specific to TRP channels and, based on insight from recent TRPV1 structures, we suggest a model of TRP channel gating that differs substantially from the one mediating voltage sensitivity in Kv channels. The common mechanism underlying polymodal gating involves the displacement of a defect in the H-bond network of S6 that changes the orientation of the pore-lining residues at the hydrophobic gate.
dc.format.extent37-50
dc.language.isoen
dc.relation.haspartJournal of General Physiology
dc.relation.isreferencedbyRockefeller University Press
dc.rightsCC BY-NC-SA
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/
dc.subjectAllosteric Regulation
dc.subjectAmino Acid Sequence
dc.subjectConserved Sequence
dc.subjectIon Channel Gating
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectPotassium Channels
dc.subjectSequence Analysis
dc.subjectTransient Receptor Potential Channels
dc.titleComparative sequence analysis suggests a conserved gating mechanism for TRP channels
dc.typeArticle
dc.type.genreJournal Article
dc.relation.doi10.1085/jgp.201411329
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.creator.orcidCarnevale, Vincenzo|0000-0002-0447-1278
dc.date.updated2021-01-31T16:19:57Z
refterms.dateFOA2021-01-31T16:20:01Z


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