Article
The pore structure and gating mechanism of K2P channels.
The EMBO journal - 5 Aug 2011
Piechotta Paula L, Rapedius Markus, Stansfeld Phillip J, Bollepalli Murali K, Ehrlich Gunter, Erhlich Gunter, Andres-Enguix Isabelle, Fritzenschaft Hariolf, Decher Niels, Sansom Mark S P, Tucker Stephen J, Baukrowitz Thomas
Abstract excerpt
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...
Topics
- Animals
- Binding Sites
- Humans
- Ion Channel Gating
- Mutation
- Porosity
- Potassium Channel Blockers
- Potassium Channels, Tandem Pore Domain
- Protein Conformation
- Quaternary Ammonium Compounds
- Rats