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dc.contributor.authorDolino, Drew M.
Chatterjee, Sudeshna
MacLean, David M.
Flatebo, Charlotte
Bishop, Logan D.C.
Shaikh, Sana A.
Landes, Christy F.
Jayaraman, Vasanthi
dc.date.accessioned 2019-01-09T17:21:12Z
dc.date.available 2019-01-09T17:21:12Z
dc.date.issued 2017
dc.identifier.citation Dolino, Drew M., Chatterjee, Sudeshna, MacLean, David M., et al.. "The structure–energy landscape of NMDA receptor gating." Nature Chemical Biology, 13, (2017) Springer Nature: 1232-1238. https://doi.org/10.1038/nchembio.2487.
dc.identifier.urihttps://hdl.handle.net/1911/105027
dc.description.abstract N-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.
dc.language.iso eng
dc.publisher Springer Nature
dc.rights This is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.
dc.title The structure–energy landscape of NMDA receptor gating
dc.type Journal article
dc.citation.journalTitle Nature Chemical Biology
dc.citation.volumeNumber 13
dc.identifier.digital nihms902663
dc.type.dcmi Text
dc.identifier.doihttps://doi.org/10.1038/nchembio.2487
dc.identifier.pmcid PMC5698143
dc.identifier.pmid 28991238
dc.type.publication post-print
dc.citation.firstpage 1232
dc.citation.lastpage 1238


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