Cryo-EM structure of TRPC5 at 2.8-Å resolution reveals unique and conserved structural elements essential for channel function | Zendy

Jingjing Duan | Zendy; Jian Li | Zendy; Gui-Lan Chen | Zendy; Yan Ge | Zendy; Jieyu Liu | Zendy; Kechen Xie | Zendy; Xiaogang Peng | Zendy; Wei Zhou | Zendy; Jianing Zhong | Zendy; Yixing Zhang | Zendy; Jie Xu | Zendy; Changhu Xue | Zendy; Bo Liang | Zendy; Lan Zhu | Zendy; Wei Liu | Zendy; Cheng Zhang | Zendy; XiaoLi Tian | Zendy; Jianbin Wang | Zendy; David E. Clapham | Zendy; Bo Zeng | Zendy; Zongli Li | Zendy; Jin Zhang | Zendy

Open Access

Cryo-EM structure of TRPC5 at 2.8-Å resolution reveals unique and conserved structural elements essential for channel function

Author(s) -

Jingjing Duan,

Jian Li,

Gui-Lan Chen,

Yan Ge,

Jieyu Liu,

Kechen Xie,

Xiaogang Peng,

Wei Zhou,

Jianing Zhong,

Yixing Zhang,

Jie Xu,

Changhu Xue,

Bo Liang,

Lan Zhu,

Wei Liu,

Cheng Zhang,

XiaoLi Tian,

Jianbin Wang,

David E. Clapham,

Bo Zeng,

Zongli Li,

Jin Zhang

Publication year - 2019

Publication title -

science advances

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.928

H-Index - 146

ISSN - 2375-2548

DOI - 10.1126/sciadv.aaw7935

Subject(s) - trpc5 , ion channel , structural biology , computational biology , function (biology) , biology , genetics , trpc1 , receptor

The transient receptor potential canonical subfamily member 5 (TRPC5), one of seven mammalian TRPC members, is a nonselective calcium-permeant cation channel. TRPC5 is of considerable interest as a drug target in the treatment of progressive kidney disease, depression, and anxiety. Here, we present the 2.8-Å resolution cryo-electron microscopy (cryo-EM) structure of the mouse TRPC5 (mTRPC5) homotetramer. Comparison of the TRPC5 structure to previously determined structures of other TRPC and TRP channels reveals differences in the extracellular pore domain and in the length of the S3 helix. The disulfide bond at the extracellular side of the pore and a preceding small loop are essential elements for its proper function. This high-resolution structure of mTRPC5, combined with electrophysiology and mutagenesis, provides insight into the lipid modulation and gating mechanisms of the TRPC family of ion channels.

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