Structural properties determining low K+ affinity of the selectivity filter in the TWIK1 K+ channel
نویسندگان
چکیده
منابع مشابه
Initial steps of inactivation at the K+ channel selectivity filter.
K(+) efflux through K(+) channels can be controlled by C-type inactivation, which is thought to arise from a conformational change near the channel's selectivity filter. Inactivation is modulated by ion binding near the selectivity filter; however, the molecular forces that initiate inactivation remain unclear. We probe these driving forces by electrophysiology and molecular simulation of MthK,...
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Molecular dynamics simulations of a bacterial potassium channel (KcsA) embedded in a phospholipid bilayer reveal significant differences in interactions of the selectivity filter with K(+) compared with Na(+) ions. K(+) ions and water molecules within the filter undergo concerted single-file motion in which they translocate between adjacent sites within the filter on a nanosecond timescale. In ...
متن کاملMechanism of activation at the selectivity filter of the KcsA K+ channel
Potassium channels are opened by ligands and/or membrane potential. In voltage-gated K+ channels and the prokaryotic KcsA channel, conduction is believed to result from opening of an intracellular constriction that prevents ion entry into the pore. On the other hand, numerous ligand-gated K+ channels lack such gate, suggesting that they may be activated by a change within the selectivity filter...
متن کاملVoltage-dependent inactivation gating at the selectivity filter of the MthK K+ channel
Voltage-dependent K(+) channels can undergo a gating process known as C-type inactivation, which involves entry into a nonconducting state through conformational changes near the channel's selectivity filter. C-type inactivation may involve movements of transmembrane voltage sensor domains, although the mechanisms underlying this form of inactivation may be heterogeneous and are often unclear. ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2018
ISSN: 0021-9258
DOI: 10.1074/jbc.ra118.001817