Key result
Automated docking and molecular dynamics simulations showed that TEA forms stable complexes at both the external and internal entrances of the KcsA potassium channel selectivity filter.
Molecular dynamics simulations reveal that TEA forms stable complexes at both entrances of the KcsA selectivity filter, with the Y82V mutation reducing external binding affinity due to loss of hydrophobic interactions.
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May guide K+ channel modulator design; leaves open validation in mammalian cardiac models.
Luzhkov et al. (2001) studied this question. Tetraethylammonium (TEA) was evaluated on Binding modes and energies for TEA binding at the external and internal sides of the channel pore. Automated docking and molecular dynamics simulations showed that TEA forms stable complexes at both the external and internal entrances of the KcsA potassium channel selectivity filter.
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