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- W2024358879 endingPage "942" @default.
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- W2024358879 abstract "The active site of voltage-activated potassium channels is a transmembrane aqueous pore that permits ions to permeate the cell membrane in a rapid yet highly selective manner. A useful probe for the pore of potassium-selective channels is the organic ion tetraethylammonium (TEA), which binds with millimolar affinity to the intracellular opening of the pore and blocks potassium current. In the potassium channel encoded by the Drosophila Shaker gene, an amino acid residue that specifically affects the affinity for intracellular TEA has now been identified by site-directed mutagenesis. This residue is in the middle of a conserved stretch of 18 amino acids that separates two locations that are both near the external opening of the pore. These findings suggest that this conserved region is intimately involved in the formation of the ion conduction pore of voltage-activated potassium channels. Further, a stretch of only eight amino acid residues must traverse 80 percent of the transmembrane electric potential difference." @default.
- W2024358879 created "2016-06-24" @default.
- W2024358879 creator A5021381186 @default.
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- W2024358879 date "1991-02-22" @default.
- W2024358879 modified "2023-09-27" @default.
- W2024358879 title "Mutations Affecting Internal TEA Blockade Identify the Probable Pore-Forming Region of a K <sup>+</sup> Channel" @default.
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- W2024358879 doi "https://doi.org/10.1126/science.2000494" @default.
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