Feng Zhou

Northwestern Polytechnical University

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Yu Rao

Tsinghua University

Bo Huang

Beijing Haidian Hospital

Daohua Jiang

Institute of Physics

Mingxia Gao

Fudan University

Xu Li

Kennedy Krieger Institute

Wei Xie

Center for Life Sciences

Jianjun Yang

Air Force Medical University

Roger R. Reddel

University of Sydney

Charles Pineau

Musée de l'Homme

Zemin Zhang

Center for Life Sciences

Cooperative Institutions

Chinese Academy of Sciences

University of Chinese Academy of Sciences

Chinese Academy of Medical Sciences & Peking Union Medical College

Peking University

Beijing Proteome Research Center

Sun Yat-sen University

Chinese PLA General Hospital

Fudan University

Shanghai Jiao Tong University

Shanghai Institute of Materia Medica

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π-HuB: the proteomic navigator of the human body

Nature (2024)

Fuchu He Ruedi Aebersold Mark S. Baker Xiu‐Wu Bian Xiaochen Bo

Human proteome project

Human body

10.1038/s41586-024-08280-5

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Citations (5)

Stimuli-activatable PROTACs for precise protein degradation and cancer therapy

Science Bulletin (2023)

Jing Gao Lei Yang Shumin Lei Feng Zhou Hui-Jun Nie

Protein Degradation

Proteolysis

10.1016/j.scib.2023.04.028

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Citations (31)

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

Nature Communications (2023)

Yue Li Tian Yuan Bo Huang Feng Zhou Chao Peng

The sodium channel NaV1.6 is widely expressed in neurons of the central and peripheral nervous systems, which plays a critical role in regulating neuronal excitability. Dysfunction of NaV1.6 has been linked to epileptic encephalopathy, intellectual disability and movement disorders. Here we present cryo-EM structures of human NaV1.6/β1/β2 alone and complexed with a guanidinium neurotoxin 4,9-anhydro-tetrodotoxin (4,9-ah-TTX), revealing molecular mechanism of NaV1.6 inhibition by the blocker. The apo-form structure reveals two potential Na+ binding sites within the selectivity filter, suggesting a possible mechanism for Na+ selectivity and conductance. In the 4,9-ah-TTX bound structure, 4,9-ah-TTX binds to a pocket similar to the tetrodotoxin (TTX) binding site, which occupies the Na+ binding sites and completely blocks the channel. Molecular dynamics simulation results show that subtle conformational differences in the selectivity filter affect the affinity of TTX analogues. Taken together, our results provide important insights into NaV1.6 structure, ion conductance, and inhibition.

NAV1

Tetrodotoxin

Nav1.5

Sodium channel blocker

10.1038/s41467-023-36766-9

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Citations (18)

Prediction of building energy consumption for public structures utilizing BIM-DB and RF-LSTM

Energy Reports (2024)

Feng Zhou Chengdong Yang Zhe Wang

Consumption

10.1016/j.egyr.2024.10.044