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1
Published in 2019 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.9b01092
Abstract: In potassium (K+) channels, permeation, selectivity, and gating at the selectivity filter are all governed by the thermodynamics and kinetics of the ion-protein interactions. Specific contacts between the carbonyl groups from the Thr-Val-Gly-Tyr-Gly signature filter…
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Keywords:
ion binding;
binding sites;
ion;
kcsa ... See more keywords
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2
Published in 2023 at "Biomedicines"
DOI: 10.3390/biomedicines11051376
Abstract: Here, we report an allosteric effect of an anionic phospholipid on a model K+ channel, KcsA. The anionic lipid in mixed detergent–lipid micelles specifically induces a change in the conformational equilibrium of the channel selectivity…
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Keywords:
kcsa;
conformational equilibrium;
anionic lipid;
selectivity filter ... See more keywords
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1
Published in 2020 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms21072554
Abstract: KcsA, a prokaryote tetrameric potassium channel, was the first ion channel ever to be structurally solved at high resolution. This, along with the ease of its expression and purification, made KcsA an experimental system of…
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Keywords:
protein;
lipid binding;
channel;
structure ... See more keywords
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1
Published in 2021 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms222111954
Abstract: The allosteric coupling between activation and inactivation processes is a common feature observed in K+ channels. Particularly, in the prokaryotic KcsA channel the K+ conduction process is controlled by the inner gate, which is activated…
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Keywords:
homo fret;
homo;
gate;
fret measurements ... See more keywords