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• W1991230688 endingPage "e1002476" @default.
• W1991230688 startingPage "e1002476" @default.
• W1991230688 abstract "Voltage-gated Na⁺-channels are transmembrane proteins that are responsible for the fast depolarizing phase of the action potential in nerve and muscular cells. Selective permeability of Na⁺ over Ca²⁺ or K⁺ ions is essential for the biological function of Na⁺-channels. After the emergence of the first high-resolution structure of a Na⁺-channel, an anionic coordination site was proposed to confer Na⁺ selectivity through partial dehydration of Na⁺ via its direct interaction with conserved glutamate side chains. By combining molecular dynamics simulations and free-energy calculations, a low-energy permeation pathway for Na⁺ ion translocation through the selectivity filter of the recently determined crystal structure of a prokaryotic sodium channel from Arcobacter butzleri is characterised. The picture that emerges is that of a pore preferentially occupied by two ions, which can switch between different configurations by crossing low free-energy barriers. In contrast to K⁺-channels, the movements of the ions appear to be weakly coupled in Na⁺-channels. When the free-energy maps for Na⁺ and K⁺ ions are compared, a selective site is characterised in the narrowest region of the filter, where a hydrated Na⁺ ion, and not a hydrated K⁺ ion, is energetically stable." @default.
• W1991230688 created "2016-06-24" @default.
• W1991230688 creator A5022820593 @default.
• W1991230688 creator A5074261138 @default.
• W1991230688 date "2012-04-05" @default.
• W1991230688 modified "2023-09-30" @default.
• W1991230688 title "On Conduction in a Bacterial Sodium Channel" @default.
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• W1991230688 doi "https://doi.org/10.1371/journal.pcbi.1002476" @default.
• W1991230688 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3320569" @default.
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