The pore structure and gating mechanism of K2P channels.

Journal article

Two-pore domain (K2P) potassium channels are important regulators of cellular electrical excitability. However, the structure of these channels and their gating mechanism, in particular the role of the bundle-crossing gate, are not well understood. Here, we report that quaternary ammonium (QA) ions bind with high-affinity deep within the pore of TREK-1 and have free access to their binding site before channel activation by intracellular pH or pressure. This demonstrates that, unlike most othe...

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Authors: Piechotta, P; Rapedius, M; Stansfeld, P; Bollepalli, M; Ehrlich, G

• Publication status: Published
• Journal: EMBO journal
• Volume: 30
• Issue: 17
• Pages: 3607-3619
• Publication date: 2011-08-01
• DOI: 10.1038/emboj.2011.268
• EISSN: 1460-2075
• ISSN: 0261-4189
• Language: English
• Keywords: Porosity; Rats; Potassium Channel Blockers; Humans; Potassium Channels, Tandem Pore Domain; Quaternary Ammonium Compounds; Mutation; Binding Sites; Ion Channel Gating; Protein Conformation; Animals