trpv2 channel has a similar structure to potassium channels, which are the largest ion channel family. this channel is composed of six transmembrane spanning regions (s1-s6) with a pore forming loop between s5 and s6. the pore forming loop also defines the selectivity filter, which determines the ions that are able to enter the channel. the s1-s4 region, as well as the n and c terminals of the protein, is important in reference to the gating of the channel. although trpv2 is a nonspecific cation channel, it is more permeable to calcium ions; calcium is an intracellular messenger and plays a very important role in a variety of different cellular processes. at rest, the pore channel is closed; in the activated state, the channel opens, allowing the influx of sodium and calcium ions that initiates an action potential.