4I9W

Human two pore domain K+ channel TRAAK (K2P4.1) - Fab complex structure

4I9W の概要

• エントリーDOI: 10.2210/pdb4i9w/pdb
• 分子名称: Potassium channel subfamily K member 4, ANTIBODY FAB FRAGMENT LIGHT CHAIN, ANTIBODY FAB FRAGMENT HEAVY CHAIN, ... (6 entities in total)
• 機能のキーワード: potassium ion channel, metal transport
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Multi-pass membrane protein (Potential): Q9NYG8
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 160472.83

構造登録者

Brohawn, S.G.,Mackinnon, R. (登録日: 2012-12-05, 公開日: 2013-01-23, 最終更新日: 2024-11-06)

主引用文献

Brohawn, S.G.,Campbell, E.B.,Mackinnon, R.
Domain-swapped chain connectivity and gated membrane access in a Fab-mediated crystal of the human TRAAK K+ channel.
Proc.Natl.Acad.Sci.USA, 110:2129-2134, 2013

PubMed Abstract: TRAAK (TWIK-related arachidonic acid-stimulated K(+) channel, K2P4.1) K(+) ion channels are expressed predominantly in the nervous system to control cellular resting membrane potential and are regulated by mechanical and chemical properties of the lipid membrane. TRAAK channels are twofold symmetric, which precludes a direct extension of gating mechanisms that close canonical fourfold symmetric K(+) channels. We present the crystal structure of human TRAAK in complex with antibody antigen-binding fragments (Fabs) at 2.75-Å resolution. In contrast to a previous structure, this structure reveals a domain-swapped chain connectivity enabled by the helical cap that exchanges two opposing outer helices 180° around the channel. An unrelated conformational change of an inner helix seals a side opening to the membrane bilayer and is associated with structural changes around the K(+)-selectivity filter that may have implications for mechanosensitivity and gating of TRAAK channels.

PubMed: 23341632
DOI: 10.1073/pnas.1218950110

実験手法

X-RAY DIFFRACTION (2.75 Å)