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• W3120964674 abstract "Abstract Voltage-gated potassium (K V ) channels can be opened by negatively charged resin acids and their derivatives. These resin acids have been proposed to attract the positively charged voltage-sensor helix (S4) toward the extracellular side of the membrane by binding to a pocket located between the lipid-facing extracellular ends of the transmembrane segments S3 and S4. By contrast to this proposed mechanism, neutralization of the top gating charge of the Shaker K V channel increased resin-acid induced opening, suggesting other mechanisms and sites of action. Here we explored the binding of two resin-acid derivatives, Wu50 and Wu161, to the activated/open state of the Shaker K V channel by a combination of in-silico docking, molecular dynamics simulations, and electrophysiology of mutated channels. We identified three potential resin-acid binding sites around S4: (1) The S3/S4 site previously suggested, in which positively charged residues introduced at the top of S4 are critical to keep the compound bound, (2) a site in the cleft between S4 and the pore domain (S4/pore site), in which a tryptophan at the top of S6 and the top gating charge of S4 keeps the compound bound, and (3) a site located on the extracellular side of the voltage-sensor domain, in a cleft formed by S1-S4 (the top-VSD site). The multiple binding sites around S4 and the anticipated helical-screw motion of the helix during activation make the effect of resin-acid derivatives on channel function intricate. The propensity of a specific resin acid to activate and open a voltage-gated channel likely depends on its exact binding dynamics and the types of interactions it can form with the protein in a state-specific manner. eTOC Summary Silverå Ejneby et al use molecular dynamics simulations and electrophysiology to show that the voltage-gated Shaker potassium channel has multiple binding sites for resin-acid derivatives that can regulate its opening." @default.
• W3120964674 created "2021-01-18" @default.
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• W3120964674 date "2020-06-12" @default.
• W3120964674 modified "2023-10-18" @default.
• W3120964674 title "Resin-acid derivatives bind to multiple sites on the voltage-sensor domain of the Saker channel" @default.
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• W3120964674 doi "https://doi.org/10.1101/2020.06.11.146548" @default.
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