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- W2031444513 abstract "The conductance of potassium channels can be regulated by C-type inactivation, which consists in the time-dependent closing of their selectivity filter following activation. Crystallization of the KcsA channel from S. lividans under conditions of low potassium concentration revealed conformational changes of the selectivity filter preventing the permeation of both K and Na ions. This structure was associated with the C-type inactivated state of K channels. Under similar low potassium crystallization conditions, MthK from M. thermoautotrophicum, another model potassium channel, remains in its canonical conductive state. Functional studies nevertheless show that MthK undergo C-type inactivation like KcsA. In KcsA, the transition to the inactivated state is favored by a glutamate in the vicinity of the selectivity filter (Glu71). Mutation of this residue to alanine decreases inactivation drastically. Our electrophysiology and molecular simulation data show that, in MthK, a mutation of a valine at the same position to a glutamate (V55E) accelerates inactivation and results in a conformation of the selectivity filter similar to the inactivated state of KcsA. These results support the idea that potassium channels can potentially adopt two different inactivated states. We further investigate changes in ion binding affinity in MthK and KcsA channel mutants to understand the underlying difference in inactivation behavior using molecular dynamic simulations, free energy calculations and electrophysiological measurements." @default.
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- W2031444513 date "2014-01-01" @default.
- W2031444513 modified "2023-09-28" @default.
- W2031444513 title "Microscopic Mechanisms Underlying Inactivation in the KcsA and MTHK K+ Channels" @default.
- W2031444513 doi "https://doi.org/10.1016/j.bpj.2013.11.3021" @default.
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