+Search query
-Structure paper
Title | Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes. |
---|---|
Journal, issue, pages | Elife, Vol. 8, Year 2019 |
Publish date | May 15, 2019 |
Authors | Lejla Zubcevic / Allen L Hsu / Mario J Borgnia / Seok-Yong Lee / |
PubMed Abstract | 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 ...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. |
External links | Elife / PubMed:31090543 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.9 - 4.2 Å |
Structure data | EMDB-20143, PDB-6oo3: EMDB-20145, PDB-6oo4: EMDB-20146, PDB-6oo5: EMDB-20148, PDB-6oo7: |
Chemicals | ChemComp-6EU: |
Source |
|
Keywords | METAL TRANSPORT / ion channel / calcium channel / TRP channel |