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dc.contributor.authorBagnéris, Claireen_US
dc.contributor.authorDeCaen, Paul G.en_US
dc.contributor.authorHall, Benjamin A.en_US
dc.contributor.authorNaylor, Claire E.en_US
dc.contributor.authorClapham, David E.en_US
dc.contributor.authorKay, Christopher W. M.en_US
dc.contributor.authorWallace, B. A.en_US
dc.date.accessioned2014-03-10T20:32:38Z
dc.date.issued2013en_US
dc.identifier.citationBagnéris, Claire, Paul G. DeCaen, Benjamin A. Hall, Claire E. Naylor, David E. Clapham, Christopher W. M. Kay, and B. A. Wallace. 2013. “Role of the C-terminal domain in the structure and function of tetrameric sodium channels.” Nature Communications 4 (1): 2465. doi:10.1038/ncomms3465. http://dx.doi.org/10.1038/ncomms3465.en
dc.identifier.issn2041-1723en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:11878805
dc.description.abstractVoltage-gated sodium channels have essential roles in electrical signalling. Prokaryotic sodium channels are tetramers consisting of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain. Previous crystal structures of bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs). Here, using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we show that the CTD of the NavMs channel from Magnetococcus marinus includes a flexible region linking the TM domains to a four-helix coiled-coil bundle. A 2.9 Å resolution crystal structure of the NavMs pore indicates the position of the CTD, which is consistent with the EPR-derived structure. Functional analyses demonstrate that the coiled-coil domain couples inactivation with channel opening, and is enabled by negatively charged residues in the linker region. A mechanism for gating is proposed based on the structure, whereby splaying of the bottom of the pore is possible without requiring unravelling of the coiled-coil.en
dc.language.isoen_USen
dc.publisherNature Pub. Groupen
dc.relation.isversionofdoi:10.1038/ncomms3465en
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791462/pdf/en
dash.licenseLAAen_US
dc.titleRole of the C-terminal domain in the structure and function of tetrameric sodium channelsen
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden
dc.relation.journalNature Communicationsen
dash.depositing.authorDeCaen, Paul G.en_US
dc.date.available2014-03-10T20:32:38Z
dc.identifier.doi10.1038/ncomms3465*
dash.contributor.affiliatedDeCaen, Paul
dash.contributor.affiliatedClapham, David


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