8J7H

ion channel

8J7H の概要

• エントリーDOI: 10.2210/pdb8j7h/pdb
• EMDBエントリー: 36041
• 分子名称: ion channel, ILE-ALA-ALA-ILE-HIS-ASN-ALA-ARG-ARG-LYS-LYS-ARG-GLU-ALA-ALA-ALA-ALA-HIS-LYS-ALA (3 entities in total)
• 機能のキーワード: ion channel, transport protein
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 368929.46

構造登録者

Chen, H.W.,Jiang, D. (登録日: 2023-04-27, 公開日: 2024-05-01, 最終更新日: 2025-07-02)

主引用文献

Chen, H.,Xia, Z.,Dong, J.,Huang, B.,Zhang, J.,Zhou, F.,Yan, R.,Shi, Y.,Gong, J.,Jiang, J.,Huang, Z.,Jiang, D.
Structural mechanism of voltage-gated sodium channel slow inactivation.
Nat Commun, 15:3691-3691, 2024

PubMed Abstract: Voltage-gated sodium (Na) channels mediate a plethora of electrical activities. Na channels govern cellular excitability in response to depolarizing stimuli. Inactivation is an intrinsic property of Na channels that regulates cellular excitability by controlling the channel availability. The fast inactivation, mediated by the Ile-Phe-Met (IFM) motif and the N-terminal helix (N-helix), has been well-characterized. However, the molecular mechanism underlying Na channel slow inactivation remains elusive. Here, we demonstrate that the removal of the N-helix of NaEh (NaEh) results in a slow-inactivated channel, and present cryo-EM structure of NaEh in a potential slow-inactivated state. The structure features a closed activation gate and a dilated selectivity filter (SF), indicating that the upper SF and the inner gate could serve as a gate for slow inactivation. In comparison to the NaEh structure, NaEh undergoes marked conformational shifts on the intracellular side. Together, our results provide important mechanistic insights into Na channel slow inactivation.

PubMed: 38693179
DOI: 10.1038/s41467-024-48125-3

実験手法

ELECTRON MICROSCOPY (3.3 Å)