(a) A close-up view of the linker domain. The domain has two distinct regions: the helix-loop-helix (HLH) region and the β sheet region. CTD that covers the linker domain is omitted for clarity. (b) Close-up view of the intersubunit interactions formed by the β sheet region of the linker domain. The linker domain interacts with ankyrin repeats 3 and 4 of the neighboring subunit. Dashed line represents the missing segment of the finger 3. The distal part of the CTD contributes a β strand to the β sheet of the linker domain. (c) Superposition of the rat TRPV2 ARD (magenta, PDB 2ETA) with the ARD of the rabbit TRPV2 structure (blue). The two structures diverge around the ankyrin repeat 1 and the fingers 1-3. (d) A close-up view of the coupling domain and the TRP domain with the arginine and lysine residues displayed as sticks and marked with circles. The map covering the CTD was of lower quality compared to the rest of the molecue which prevented the building of all side-chains. Where side-chains of the Arg and Lys residues were not built, we display the backbone only. Arg682, which resides in CTD, is labeld as it is the residue corresponding to Arg721 in TRPV1 which has been identified as important for binding of PIP 2 .