The structure–energy landscape of NMDA receptor gating

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dc.citation.firstpage1232en_US
dc.citation.journalTitleNature Chemical Biologyen_US
dc.citation.lastpage1238en_US
dc.citation.volumeNumber13en_US
dc.contributor.authorDolino, Drew M.en_US
dc.contributor.authorChatterjee, Sudeshnaen_US
dc.contributor.authorMacLean, David M.en_US
dc.contributor.authorFlatebo, Charlotteen_US
dc.contributor.authorBishop, Logan D.C.en_US
dc.contributor.authorShaikh, Sana A.en_US
dc.contributor.authorLandes, Christy F.en_US
dc.contributor.authorJayaraman, Vasanthien_US
dc.date.accessioned2019-01-09T17:21:12Zen_US
dc.date.available2019-01-09T17:21:12Zen_US
dc.date.issued2017en_US
dc.description.abstractN-Methyl-D-aspartate (NMDA) receptors are the main calcium-permeable excitatory receptors in the mammalian central nervous system. The NMDA receptor gating is complex, exhibiting multiple closed, open, and desensitized states; however, central questions regarding the conformations and energetics of the transmembrane domains as they relate to the gating states are still unanswered. Here, using single-molecule Förster resonance energy transfer (smFRET), we map the energy landscape of the first transmembrane segment of the Rattus norvegicus NMDA receptor under resting and various liganded conditions. These results show kinetically and structurally distinct changes associated with apo, agonist-bound, and inhibited receptors linked by a linear mechanism of gating at this site. Furthermore, the smFRET data suggest that allosteric inhibition by zinc occurs by an uncoupling of the agonist-induced changes at the extracellular domains from the gating motions leading to an apo-like state, while dizocilpine, a pore blocker, stabilizes multiple closely packed transmembrane states.en_US
dc.identifier.citationDolino, Drew M., Chatterjee, Sudeshna, MacLean, David M., et al.. "The structure–energy landscape of NMDA receptor gating." <i>Nature Chemical Biology,</i> 13, (2017) Springer Nature: 1232-1238. https://doi.org/10.1038/nchembio.2487.en_US
dc.identifier.digitalnihms902663en_US
dc.identifier.doihttps://doi.org/10.1038/nchembio.2487en_US
dc.identifier.urihttps://hdl.handle.net/1911/105027en_US
dc.language.isoengen_US
dc.publisherSpringer Natureen_US
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.en_US
dc.titleThe structure–energy landscape of NMDA receptor gatingen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpost-printen_US
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