2K7M

Structure of the Connexin40 Carboxyl terminal Domain

2K7M の概要

• エントリーDOI: 10.2210/pdb2k7m/pdb
• 分子名称: Gap junction alpha-5 protein (1 entity in total)
• 機能のキーワード: protein, gap junction, cell junction, cell membrane, membrane, transmembrane, membrane protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P28234
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11959.02

構造登録者

Bouvier, D.,Spagnol, G.,Kieken, F.,Vitrac, H.,Kellezi, A.,Forge, V. (登録日: 2008-08-14, 公開日: 2009-07-28, 最終更新日: 2024-05-22)

主引用文献

Bouvier, D.,Spagnol, G.,Chenavas, S.,Kieken, F.,Vitrac, H.,Brownell, S.,Kellezi, A.,Forge, V.,Sorgen, P.L.
Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains.
J.Biol.Chem., 284:34257-34271, 2009

PubMed Abstract: Gap junctions are intercellular channels that allow the passage of ions, small molecules, and second messengers that are essential for the coordination of cellular function. They are formed by two hemichannels, each constituted by the oligomerization of six connexins (Cx). Among the 21 different human Cx isoforms, studies have suggested that in the heart, Cx40 and Cx43 can oligomerize to form heteromeric hemichannels. The mechanism of heteromeric channel regulation has not been clearly defined. Tissue ischemia leads to intracellular acidification and closure of Cx43 and Cx40 homomeric channels. However, coexpression of Cx40 and Cx43 in Xenopus oocytes enhances the pH sensitivity of the channel. This phenomenon requires the carboxyl-terminal (CT) part of both connexins. In this study we used different biophysical methods to determine the structure of the Cx40CT and characterize the Cx40CT/Cx43CT interaction. Our results revealed that the Cx40CT is an intrinsically disordered protein similar to the Cx43CT and that the Cx40CT and Cx43CT can interact. Additionally, we have identified an interaction between the Cx40CT and the cytoplasmic loop of Cx40 as well as between the Cx40CT and the cytoplasmic loop of Cx43 (and vice versa). Our studies support the "particle-receptor" model for pH gating of Cx40 and Cx43 gap junction channels and suggest that interactions between cytoplasmic regulatory domains (both homo- and hetero-connexin) could be important for the regulation of heteromeric channels.

PubMed: 19808665
DOI: 10.1074/jbc.M109.039594

実験手法

SOLUTION NMR