Structures of a mammalian TRPM8 in closed state

Cheng Zhao; Yuan Xie; Lizhen Xu; Fan Ye; Ximing Xu; Wei Yang; Fan Yang; Jiangtao Guo

doi:10.1038/s41467-022-30919-y

Nature Communications (Jun 2022)

Structures of a mammalian TRPM8 in closed state

Cheng Zhao,
Yuan Xie,
Lizhen Xu,
Fan Ye,
Ximing Xu,
Wei Yang,
Fan Yang,
Jiangtao Guo

Affiliations

Cheng Zhao: Department of Biophysics, and Department of Neurology of the Fourth Affiliated Hospital, Zhejiang University School of Medicine
Yuan Xie: Department of Neurosurgery, Xijing Hospital, Fourth Military Medical University
Lizhen Xu: Department of Biophysics and Kidney Disease Center, The First Affiliated Hospital, Zhejiang University School of Medicine
Fan Ye: Department of Biophysics, and Department of Neurology of the Fourth Affiliated Hospital, Zhejiang University School of Medicine
Ximing Xu: Key Laboratory of Marine Drugs of Ministry of Education, School of Medicine and Pharmacy, Ocean University of China
Wei Yang: Department of Biophysics, and Department of Neurology of the Fourth Affiliated Hospital, Zhejiang University School of Medicine
Fan Yang: Department of Biophysics and Kidney Disease Center, The First Affiliated Hospital, Zhejiang University School of Medicine
Jiangtao Guo: Department of Biophysics, and Department of Neurology of the Fourth Affiliated Hospital, Zhejiang University School of Medicine

DOI: https://doi.org/10.1038/s41467-022-30919-y
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 11

Abstract

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The mechanism of cold-activated TRPM8 channel activation remains unclear. Here, authors have determined structures of mouse TRPM8 in apo or ligand-bound states, providing insights into the activation of TRPM8 structures in different states.

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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