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The complete structure of an activated open sodium channel.

<div class='caption-title'>Structure of the NavMs channel.</div>
<div class='caption-title'>Comparisons of voltage sensors.</div>
<div class='caption-title'>Comparisons of pore sizes and gates.</div>
Sula A, Booker J, Ng LC, Naylor CE, DeCaen PG, Wallace BA
OpenAccess logo Nat Commun 8 14205 (2017)
Related entries: 3zjz, 5hvx

Cited: 73 times
EuropePMC logo PMID: 28205548

Abstract

Voltage-gated sodium channels (Navs) play essential roles in excitable tissues, with their activation and opening resulting in the initial phase of the action potential. The cycling of Navs through open, closed and inactivated states, and their closely choreographed relationships with the activities of other ion channels lead to exquisite control of intracellular ion concentrations in both prokaryotes and eukaryotes. Here we present the 2.45 Å resolution crystal structure of the complete NavMs prokaryotic sodium channel in a fully open conformation. A canonical activated conformation of the voltage sensor S4 helix, an open selectivity filter leading to an open activation gate at the intracellular membrane surface and the intracellular C-terminal domain are visible in the structure. It includes a heretofore unseen interaction motif between W77 of S3, the S4-S5 interdomain linker, and the C-terminus, which is associated with regulation of opening and closing of the intracellular gate.

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  2. The complete structure of an activated open sodium channel. Sula A, Booker J, Ng LC, Naylor CE, DeCaen PG, Wallace BA. Nat Commun 8 14205 (2017)
  3. Valproic acid interactions with the NavMs voltage-gated sodium channel. Zanatta G, Sula A, Miles AJ, Ng LCT, Torella R, Pryde DC, DeCaen PG, Wallace BA. Proc Natl Acad Sci U S A 116 26549-26554 (2019)
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