Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes.
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The Transient Receptor Potential Vanilloid 2 (TRPV2) channel is a member of the temperature-sensing thermoTRPV family. Recent advances in cryo-electronmicroscopy (cryo-EM) and X-ray crystallography have provided many important insights into the gating mechanisms of thermoTRPV channels. Interestingly, crystallographic studies of ligand-dependent TRPV2 gating have shown that the TRPV2 channel adopts two-fold symmetric arrangements during the gating cycle. However, it was unclear if crystal packing forces played a role in stabilizing the two-fold symmetric arrangement of the channel. Here, we employ cryo-EM to elucidate the structure of full-length rabbit TRPV2 in complex with the agonist resiniferatoxin (RTx) in nanodiscs and amphipol. We show that RTx induces two-fold symmetric conformations of TRPV2 in both environments. However, the two-fold symmetry is more pronounced in the native-like lipid environment of the nanodiscs. Our data offers insights into a gating pathway in TRPV2 involving symmetry transitions.
SubjectCa2+ permeable channel
heat sensing ion channel
ligand gated ion channel
Published Version (Please cite this version)10.7554/eLife.45779
Publication InfoLee, Seok-Yong; Zubcevic, Lejla; Hsu, Allen L; & Borgnia, Mario J (2019). Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes. eLife, 8. 10.7554/eLife.45779. Retrieved from https://hdl.handle.net/10161/19159.
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