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- W1967411204 abstract "The mechanism of selectivity in potassium channels has been extensively studied using the prokaryotic potassium channel, KcsA. Computational studies suggest that a glutamate-aspartate H-bond behind the selectivity filter in KcsA may play a role in determining the permeation properties of the channel. However, the mutant E71A , which disrupts this H-bond interaction and abolishes pH-dependent inactivation is reported to have either no effect on K+ selectivity (1) or to increase K+ selectivity (2) as measured by reversal potentials. Using an 86Rb+ flux assay, WT KcsA exhibits strong K+ selectivity, such that there are no measurable 86Rb+ fluxes supported by Na+ and Li+. In contrast, both Na+ and Li+ support significant 86Rb+ fluxes in the E71A mutant, indicating an enhanced Na+ and Li+ permeability.In eukaryotic inward rectifying potassium channels (Kir), the E71 equivalent residue is part of a glutamate-arginine salt bridge that, when disrupted dramatically reduces K+ selectivity. KirBac1.1 is a prokaryotic channel that serves as a structural model of eukaryotic Kirs, but contains an H-bond in the equivalent position, similar to KcsA. By patch-clamping giant liposomes, we show that KirBac1.1 is K+-selective (PNa/PK < 0.08) as measured by reversal potentials shifts, but, like KcsA E71A, shows significant Na+ and Li+-driven 86Rb+ fluxes. We also find that the KcsA E71A mutant, similar to WT KirBac1.1. This loss of stability in these channels may suggest that the differences observed in permeation result from a weakened interaction with ions at the selectivity filter. Studies to examine ion permeation in eukaryotic Kir channels by 86Rb+ flux are ongoing.1. H. Choi, L. Heginbotham, Biophys.J. 86, 2137 (2004).2. J. F. Cordero-Morales et al., Nature Structural & Molecular Biology 13, 311 (2006)." @default.
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- W1967411204 date "2010-01-01" @default.
- W1967411204 modified "2023-09-26" @default.
- W1967411204 title "The E71A Mutation Alters Selective Ion Permeability in KcsA" @default.
- W1967411204 doi "https://doi.org/10.1016/j.bpj.2009.12.1800" @default.
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