Nat Struct Mol Biol

Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of \ue2\u2c6\ubc4 \uc3\u2026. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.DP2 EB020402/EB/NIBIB NIH HHS/United StatesDP2 OD008380/OD/NIH HHS/United StatesDP2EB020402/DP/NCCDPHP CDC HHS/United StatesDP2OD008380/OD/NIH HHS/United StatesR01GM100894/GM/NIGMS NIH HHS/United States2016-07-18T00:00:00Z26779611PMC487685