7CM3

Cryo-EM structure of human NALCN in complex with FAM155A

7CM3 の概要

• エントリーDOI: 10.2210/pdb7cm3/pdb
• EMDBエントリー: 30400
• 分子名称: Sodium leak channel non-selective protein, Transmembrane protein FAM155A, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: ion channel, membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 267576.20

構造登録者

Wu, J.,Yan, Z.,Ke, M. (登録日: 2020-07-24, 公開日: 2020-11-11, 最終更新日: 2025-07-02)

主引用文献

Xie, J.,Ke, M.,Xu, L.,Lin, S.,Huang, J.,Zhang, J.,Yang, F.,Wu, J.,Yan, Z.
Structure of the human sodium leak channel NALCN in complex with FAM155A.
Nat Commun, 11:5831-5831, 2020

PubMed Abstract: NALCN, a sodium leak channel expressed mainly in the central nervous system, is responsible for the resting Na permeability that controls neuronal excitability. Dysfunctions of the NALCN channelosome, NALCN with several auxiliary subunits, are associated with a variety of human diseases. Here, we report the cryo-EM structure of human NALCN in complex with FAM155A at an overall resolution of 3.1 angstroms. FAM155A forms extensive interactions with the extracellular loops of NALCN that may help stabilize NALCN in the membrane. A Na ion-binding site, reminiscent of a Ca binding site in Ca channels, is identified in the unique EEKE selectivity filter. Despite its 'leaky' nature, the channel is closed and the intracellular gate is sealed by S6, II-III linker and III-IV linker. Our study establishes the molecular basis of Na permeation and voltage sensitivity, and provides important clues to the mechanistic understanding of NALCN regulation and NALCN channelosome-related diseases.

PubMed: 33203861
DOI: 10.1038/s41467-020-19667-z

実験手法

ELECTRON MICROSCOPY (3.1 Å)