Abstract
Transient Receptor Potential (TRP) channels are a large superfamily of polymodal ion channels, which perform important roles in numerous physiological processes. The architecture of their transmembrane (TM) domains closely resembles that of voltage-gated potassium channels (K(V)). However, recent cryoEM and crystallographic studies of TRP channels have identified π-helices in functionally important regions, and it is increasingly recognized that they utilize a distinct mechanism of gating that relies on α-to-π secondary structure transitions. Here we review our current understanding of the role of π-helices in TRP channel function and their broader impact on different classes of ion channels.