Structure of human NaV1.6 channel reveals Na+ selectivity and pore blockade by 4,9-anhydro-tetrodotoxin

Yue Li; Tian Yuan; Bo Huang; Feng Zhou; Chao Peng; Xiaojing Li; Yunlong Qiu; Bei Yang; Yan Zhao; Zhuo Huang; Daohua Jiang

doi:10.1038/s41467-023-36766-9

Nature Communications (Feb 2023)

Structure of human NaV1.6 channel reveals Na+ selectivity and pore blockade by 4,9-anhydro-tetrodotoxin

Yue Li,
Tian Yuan,
Bo Huang,
Feng Zhou,
Chao Peng,
Xiaojing Li,
Yunlong Qiu,
Bei Yang,
Yan Zhao,
Zhuo Huang,
Daohua Jiang

Affiliations

Yue Li: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Tian Yuan: State Key Laboratory of Natural and Biomimetic Drugs, Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center
Bo Huang: Beijing StoneWise Technology Co Ltd.
Feng Zhou: Beijing StoneWise Technology Co Ltd.
Chao Peng: State Key Laboratory of Natural and Biomimetic Drugs, Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center
Xiaojing Li: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Yunlong Qiu: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Bei Yang: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Yan Zhao: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Zhuo Huang: State Key Laboratory of Natural and Biomimetic Drugs, Department of Molecular and Cellular Pharmacology, School of Pharmaceutical Sciences, Peking University Health Science Center
Daohua Jiang: Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences

DOI: https://doi.org/10.1038/s41467-023-36766-9
Journal volume & issue: Vol. 14, no. 1
pp. 1 – 13

Abstract

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NaV1.6 channel plays a critical role in neuronal excitability. Here, authors present human NaV1.6 structures in apo and 4,9-anhydro-tetrodotoxin bound forms, which reveal molecular mechanisms of NaV1.6 Na+ conductance and inhibition by the blocker.

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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