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• W1968301172 abstract "K+ channels conduct and regulate K+ flux across the cell membrane. Several crystal structures and biophysical studies of tetrameric ion channels have revealed many of the structural details of ion selectivity and gating. A narrow pore lined with four arrays of carbonyl groups is responsible for ion selectivity, whereas a conformational change of the four inner transmembrane helices (TM2) is involved in gating. We used NMR to examine full-length KcsA, a prototypical K+ channel, in its open, closed and intermediate states. These studies reveal that at least two conformational states exist both in the selectivity filter and near the C-terminal ends of the TM2 helices. In the ion-conducting open state, we observed rapid structural exchange between two conformations of the filter, presumably of low and high K+ affinity, respectively. Such measurements of millisecond-timescale dynamics reveal the basis for simultaneous ion selection and gating." @default.
• W1968301172 created "2016-06-24" @default.
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• W1968301172 date "2007-10-07" @default.
• W1968301172 modified "2023-10-16" @default.
• W1968301172 title "Conformational dynamics of the KcsA potassium channel governs gating properties" @default.
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• W1968301172 doi "https://doi.org/10.1038/nsmb1311" @default.
• W1968301172 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3525321" @default.
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