Abstract
SummaryTransient receptor potential vanilloid (TRPV) channels are activated by ligands and heat, and are involved in various physiological processes. In contrast to the architecturally-related voltage-gated cation channels, TRPV1 and TRPV2 subtypes possess another activation gate at the selectivity filter that can open widely enough to permeate large organic cations. Despite the advances in recent structural studies, the mechanism of selectivity filter gating and permeation of both metal ions and large molecules by TRPV1 or TRPV2 is not well known. We determined two crystal structures of rabbit TRPV2 in its Ca2+-bound and resiniferatoxin (RTx) and Ca2+-bound forms to 3.9 Å and 3.1 Å, respectively. Notably, our structures show that RTx binding leads to two-fold symmetric opening of the selectivity filter of TRPV2 that is wide enough for large organic cation permeation. Combined with functional characterizations, our studies reveal a structural basis for permeation of Ca2+ and large organic cations in TRPV2.
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