Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 11, Pages 1089-1095Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1311
Keywords
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Funding
- NIGMS NIH HHS [R01 GM056653, U54 GM074929, GM74929, GM56653] Funding Source: Medline
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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.
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