Fig. 3.

Comparison of apo TRPV3 with thermoTRPV channels. a Surface representation of the C-terminal domain (CTD) in TRPV3 compared to the CTDs in TRPV1, TRPV2, and TRPV4. The C-terminus of the CTD is resolved in TRPV3 and encircles the coupling domain (CD) β-sheet and forms an interface with the neighboring ARD (ARD⁺¹). b Comparison of selectivity filters (SF) and helix bundle gates in TRPV3 (gold), TRPV1 (cyan), TRPV2 (blue), and TRPV4 (purple). SF residues are indicated by a shaded box and shown in stick representation. Residues representing the helix bundle gate are shown in stick representation. c Overlay of the transmembrane domains (TM) of TRPV2 (marine) and TRPV3 (gold) of a single monomer. The TMs of TRPV2 are all α-helical, while the S4−S5 linker of TRPV3 contains a π-helical turn