TRPV channels share general mechanisms of activation while exhibiting subtype-specific features along the activation pathway that can determine their apparent sensitivity to stimuli.

Structure-based virtual screening reveals multiple novel TRPV5 inhibitors that bind and exert their effect from previously unidentified binding sites as characterized by cryo-electron microscopy and electrophysiology.

Structural insights into the architecture and functional properties of zebrafish TRPC4 are revealed by high-resolution cryo-EM.

Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.

The molecular identity of the temperature-sensitive ion channel of human sperm that ensures depolarization is TRPV4.

Ligand-induced two-fold symmetric arrangement in TRPV2 is observed in the native-like nanodisc-reconstituted condition using cryo-electron microscopy.

The TRPV1, TRPV2 and TRPV3 channels are gated on the cytosolic side of the pore, whereas structural changes in the ion selectivity filter associated with activation don't control cation access.

Mg²⁺-dependent JAK1-mediated phosphorylation sensitizes TRPV2 activity and thermo-threshold, which is counterbalanced by PTPN1-mediated dephosphorylation, highlighting a role of phosphorylation homeostasis in setting the basal activity of TRPV2.

Cannabidiol binds to TRPV2 via a previously unidentified, but highly conserved, pocket.

C-terminal domain of thermoTRPV channels regulates channel gating at the cytoplasmic interface through a switch-like process.