Abstract
Transient receptor potential (TRP) cation channels act as cellular sensors of a wide variety of stimuli and play a role in many biological processes, making them attractive pharmacological targets. However, the lack of specific agonists or antagonists for many subfamily members has impeded studies of both their biophysical properties and their broader biological functions. The architecture of the TRP channel transmembrane domain, which contains both the ion conducting pore and several ligand binding sites, is conserved across the family, and previous studies transferring ligand sensitivity among TRP channels revealed conserved channel gating mechanisms within the Vanilloid subfamily.
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