7CU3

Structure of mammalian NALCN-FAM155A complex at 2.65 angstrom

7CU3 の概要

• エントリーDOI: 10.2210/pdb7cu3/pdb
• EMDBエントリー: 30470
• 分子名称: Sodium leak channel non-selective protein, Transmembrane protein FAM155A, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: nalcn, channel, fam155, nca, nlf, transport protein
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 263530.72

構造登録者

Chen, L.,Kang, Y. (登録日: 2020-08-20, 公開日: 2020-11-18, 最終更新日: 2025-07-02)

主引用文献

Kang, Y.,Wu, J.X.,Chen, L.
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex.
Nat Commun, 11:6199-6199, 2020

PubMed Abstract: Resting membrane potential determines the excitability of the cell and is essential for the cellular electrical activities. The NALCN channel mediates sodium leak currents, which positively adjust resting membrane potential towards depolarization. The NALCN channel is involved in several neurological processes and has been implicated in a spectrum of neurodevelopmental diseases. Here, we report the cryo-EM structure of rat NALCN and mouse FAM155A complex to 2.7 Å resolution. The structure reveals detailed interactions between NALCN and the extracellular cysteine-rich domain of FAM155A. We find that the non-canonical architecture of NALCN selectivity filter dictates its sodium selectivity and calcium block, and that the asymmetric arrangement of two functional voltage sensors confers the modulation by membrane potential. Moreover, mutations associated with human diseases map to the domain-domain interfaces or the pore domain of NALCN, intuitively suggesting their pathological mechanisms.

PubMed: 33273469
DOI: 10.1038/s41467-020-20002-9

実験手法

ELECTRON MICROSCOPY (2.65 Å)