Membrane-bound channel proteins of the transient receptor potential (TRP) family have overall architecture similar to simple voltage gated cationic channels, consisting of four sensor domains linked to a central pore. Structural studies have yielded clues into the possible operational mechanisms of these nanomachines, including the capsaicin or vanilloid receptor, TRPV1. Molecular simulations have been employed in an attempt to shed light on the closed to open transition of TRPV1. Seemingly, gating relies on the motion of an evolutionarily conserved amino acid in the middle of a helix comprising the pore domain. On rotation, this side chain can face either the central pore or the linker, which connects the pore to the sensors. Only in the former case is the lumen hydrated and thus conductive. A model for TRPV1 gating is proposed involving the dynamic hydration of four cavities.

Wetting-dewetting transitions and nature's way of sensing pain

2019 Fall National Meeting

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