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- W2315673045 abstract "Voltage-gated potassium channels of the Kv1 family play a crucial role in the generation and transmission of electrical signals in excitable cells affecting neuronal and cardiac activities. Small-molecule blockage of these channels has been proposed to occur via a cooperative mechanism involving two main blocking sites: the inner-pore site located below the selectivity filter, and a side-pocket cavity located between the pore and the voltage sensor. Using 0.5 μs molecular dynamics simulation trajectories complemented by docking calculations, the potential binding sites of the PAP-1 (5-(4-phenoxybutoxy)psoralen) blocker to the crystal structure of Kv1.2 channel have been studied. The presence of both mentioned blocking sites at Kv1.2 is confirmed, adding evidence in favor of a cooperative channel blockage mechanism. These observations provide insight into drug modulation that will guide further developments of Kv inhibitors." @default.
- W2315673045 created "2016-06-24" @default.
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- W2315673045 date "2015-03-16" @default.
- W2315673045 modified "2023-10-16" @default.
- W2315673045 title "In Silico Identification of PAP-1 Binding Sites in the Kv1.2 Potassium Channel" @default.
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- W2315673045 doi "https://doi.org/10.1021/acs.molpharmaceut.5b00023" @default.
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