Hydrophobic plug functions as a gate in voltage-gated proton channels

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Abstract
Significance: Voltage-gated proton (Hv1) channels play important roles in various physiological processes, such as the innate immune response. However, the mechanism by which this channel closes and opens its proton permeation pathways is unknown, due to the lack of structural information about the closed and open states of the channel. This study uses both simulation and experimental approaches to develop models of the closed and open states of the Hv1 channel. These models suggest a mechanism for how the channel closes and opens. The models also suggest a mechanism explaining why a blocker only binds to the open state of the channel. These structural models will be essential for future investigations of this channel and the development of new pharmacological blockers.

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