Matches in SemOpenAlex for { <https://semopenalex.org/work/W2167272020> ?p ?o ?g. }
- W2167272020 abstract "Uniquely, the ClC family harbours dissipative channels and anion/H(+) transporters that share unprecedented functional characteristics. ClC-1 channels are homodimers in which each monomer supports an identical pore carrying three anion-binding sites. Transient occupancy of the extracellular binding site by a conserved glutamate residue, E232, independently gates each pore. A common gate, the molecular basis of which is unknown, closes both pores simultaneously. Mutations affecting common gating underlie myotonia congenita in humans. Here we show that the common gate likely occludes the channel pore via interaction of E232 with a highly conserved tyrosine, Y578, at the central anion-binding site. We also identify structural linkages important for coordination of common gating between subunits and modulation by intracellular molecules. Our data reveal important molecular determinants of common gating of ClC channels and suggest that the molecular mechanism is an evolutionary vestige of coupled anion/H(+) transport." @default.
- W2167272020 created "2016-06-24" @default.
- W2167272020 creator A5016061728 @default.
- W2167272020 creator A5066343783 @default.
- W2167272020 date "2013-09-25" @default.
- W2167272020 modified "2023-10-13" @default.
- W2167272020 title "Molecular determinants of common gating of a ClC chloride channel" @default.
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- W2167272020 doi "https://doi.org/10.1038/ncomms3507" @default.
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