7XNH

Human Cx36/GJD2 gap junction channel with pore-lining N-terminal helices in soybean lipids

7XNH の概要

• エントリーDOI: 10.2210/pdb7xnh/pdb
• EMDBエントリー: 33256 33315
• 分子名称: Gap junction delta-2 protein, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE (2 entities in total)
• 機能のキーワード: connexin 36, cx36, gap junction channel, gjd2, membrane protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 538444.80

構造登録者

Lee, S.N.,Cho, H.J.,Jeong, H.,Ryu, B.,Lee, H.J.,Lee, H.H.,Woo, J.S. (登録日: 2022-04-28, 公開日: 2023-03-22, 最終更新日: 2025-06-25)

主引用文献

Lee, S.N.,Cho, H.J.,Jeong, H.,Ryu, B.,Lee, H.J.,Kim, M.,Yoo, J.,Woo, J.S.,Lee, H.H.
Cryo-EM structures of human Cx36/GJD2 neuronal gap junction channel.
Nat Commun, 14:1347-1347, 2023

PubMed Abstract: Connexin 36 (Cx36) is responsible for signal transmission in electrical synapses by forming interneuronal gap junctions. Despite the critical role of Cx36 in normal brain function, the molecular architecture of the Cx36 gap junction channel (GJC) is unknown. Here, we determine cryo-electron microscopy structures of Cx36 GJC at 2.2-3.6 Å resolutions, revealing a dynamic equilibrium between its closed and open states. In the closed state, channel pores are obstructed by lipids, while N-terminal helices (NTHs) are excluded from the pore. In the open state with pore-lining NTHs, the pore is more acidic than those in Cx26 and Cx46/50 GJCs, explaining its strong cation selectivity. The conformational change during channel opening also includes the α-to-π-helix transition of the first transmembrane helix, which weakens the protomer-protomer interaction. Our structural analyses provide high resolution information on the conformational flexibility of Cx36 GJC and suggest a potential role of lipids in the channel gating.

PubMed: 36906653
DOI: 10.1038/s41467-023-37040-8

実験手法

ELECTRON MICROSCOPY (3.1 Å)