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• W2000871316 abstract "The ligand-gated potassium channels are stimulated by various kinds of messengers. Previous studies showed that ligand-gated potassium channels containing RCK domains (the regulator of the conductance of potassium ion) form a dimer of tetramer structure through the RCK octameric gating ring in the presence of detergent. Here, we have analyzed the structure of Kch, a channel of this type from Escherichia coli, in a lipid environment using electron crystallography. By combining information from the 3D map of the transmembrane part of the protein and docking of an atomic model of a potassium channel, we conclude that the RCK domains face the solution and that an RCK octameric gating ring arrangement does not form under our crystallization condition. Our findings may be applied to other potassium channels that have an RCK gating ring arrangement." @default.
• W2000871316 created "2016-06-24" @default.
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• W2000871316 date "2015-01-01" @default.
• W2000871316 modified "2023-10-03" @default.
• W2000871316 title "Free RCK Arrangement in Kch, a Putative Escherichia coli Potassium Channel, as Suggested by Electron Crystallography" @default.
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• W2000871316 doi "https://doi.org/10.1016/j.str.2014.10.018" @default.
• W2000871316 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25497729" @default.
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