9BTU

Human SCNN1B-SCNN1G ENaC dimers

9BTU の概要

• エントリーDOI: 10.2210/pdb9btu/pdb
• 関連するPDBエントリー: 9BLR 9BTG
• EMDBエントリー: 44896
• 分子名称: Amiloride-sensitive sodium channel subunit beta, 10D4 Fab, Amiloride-sensitive sodium channel subunit gamma, ... (7 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: 4
• 化学式量合計: 166492.80

構造登録者

Houser, A.,Baconguis, I. (登録日: 2024-05-15, 公開日: 2024-11-27, 最終更新日: 2025-02-19)

主引用文献

Houser, A.,Baconguis, I.
Structural insights into subunit-dependent functional regulation in epithelial sodium channels.
Structure, 33:349-362.e4, 2025

PubMed Abstract: Epithelial sodium channels (ENaCs) play a crucial role in Na reabsorption in mammals. To date, four subunits have been identified-α, β, γ, and δ-believed to form different heteromeric complexes. Currently, only the structure of the αβγ complex is known. To investigate the formation of channels with different subunit compositions and to determine how each subunit contributes to distinct channel properties, we co-expressed human δ, β, and γ. Using single-particle cryoelectron microscopy, we observed three distinct ENaC complexes. The structures unveil a pattern in which β and γ positions are conserved among the different complexes while the α position in αβγ trimer is occupied by either δ or another β. The δ subunit induces structural rearrangements in the γ subunit, which may contribute to the differences in channel activity between αβγ and δβγ channels. These structural changes provide molecular insights into how ENaC subunit composition modulates channel function.

PubMed: 39667931
DOI: 10.1016/j.str.2024.11.013

実験手法

ELECTRON MICROSCOPY (3.68 Å)