The complete structure of an activated open sodium channel

Altin Sula; Jennifer Booker; Leo C. T. Ng; Claire E. Naylor; Paul G. DeCaen; B. A. Wallace

doi:10.1038/ncomms14205

Nature Communications (Feb 2017)

The complete structure of an activated open sodium channel

Altin Sula,
Jennifer Booker,
Leo C. T. Ng,
Claire E. Naylor,
Paul G. DeCaen,
B. A. Wallace

Affiliations

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: Department of Pharmacology, Feinberg School of Medicine, Northwestern University
Claire E. Naylor: Institute of Structural and Molecular Biology, Birkbeck College, University of London
Paul G. DeCaen: Department of Pharmacology, Feinberg School of Medicine, Northwestern University
B. A. Wallace: Institute of Structural and Molecular Biology, Birkbeck College, University of London

DOI: https://doi.org/10.1038/ncomms14205
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 9

Abstract

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Voltage-gated sodium (Nav) channels are crucial for action potential initiation in excitable cells. Here the authors present the complete structure of prokaryotic NavMs in a fully open state, providing structural insight into the opening and closure of the channel's intracellular gate.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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