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• W2085281708 abstract "Crystallographic studies of channel proteins have provided insight into the molecular mechanisms of ion channels, even though these structures are obtained in the absence of the membrane and some structural portions have remained unsolved. Here we report the gating structure of the membrane-embedded KcsA potassium channel using atomic force microscopy (AFM). The activation gate of the KcsA channel is located on the intracellular side and the cytoplasmic domain was truncated to clear the view of this location. Once opened, the individual subunits in the tetramer were resolved with the pore open at the center. Furthermore, AFM was able to capture the previously unsolved bulge helix at the entrance. A molecular dynamics simulation revealed that the bulge helices fluctuated dramatically at the open entryway. This dynamic behavior was observed as vigorous open-channel noise in the single-channel current recordings. The role of the bulge helices in the open gate structure is discussed." @default.
• W2085281708 created "2016-06-24" @default.
• W2085281708 creator A5023979356 @default.
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• W2085281708 creator A5044989356 @default.
• W2085281708 date "2013-01-15" @default.
• W2085281708 modified "2023-09-30" @default.
• W2085281708 title "The Open Gate Structure of the Membrane-Embedded KcsA Potassium Channel Viewed From the Cytoplasmic Side" @default.
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• W2085281708 doi "https://doi.org/10.1038/srep01063" @default.
• W2085281708 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3545221" @default.
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• W2085281708 hasPublicationYear "2013" @default.
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