The complete structure of an activated open sodium channel

Altin Sula, Jennifer Booker, Leo C. T. Ng, Claire E. Naylor, Paul G. DeCaen () and B. A. Wallace ()
Additional contact information
Altin Sula: Institute of Structural and Molecular Biology, Birkbeck College, University of London
Jennifer Booker: Institute of Structural and Molecular Biology, Birkbeck College, University of London
Leo C. T. Ng: Feinberg School of Medicine, Northwestern University
Claire E. Naylor: Institute of Structural and Molecular Biology, Birkbeck College, University of London
Paul G. DeCaen: Feinberg School of Medicine, Northwestern University
B. A. Wallace: Institute of Structural and Molecular Biology, Birkbeck College, University of London

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/ncomms14205 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14205

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms14205

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().