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The complete structure of an activated open sodium channel

DOI: 10.1038/ncomms14205 DOI Help

Authors: Altin Sula (Birkbeck College, University of London) , Jennifer Booker (Birkbeck College, University of London) , Leo C. T. Ng (Feinberg School of Medicine, Northwestern University) , Claire Naylor (Birkbeck College, University of London) , Paul G. Decaen (Feinberg School of Medicine, Northwestern University) , B. A. Wallace (Birkbeck College, University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: February 2017
Diamond Proposal Number(s): 12305

Open Access Open Access

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.

Journal Keywords: Ion channels in the nervous system; Sodium channels; X-ray crystallography

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: Soleil; European Synchrotron Radiation Facility

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