6OO5
Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in amphipol resolved to 4.2 A
Summary for 6OO5
| Entry DOI | 10.2210/pdb6oo5/pdb |
| EMDB information | 20143 20145 20146 20148 |
| Descriptor | TRPV2, resiniferatoxin (2 entities in total) |
| Functional Keywords | ion channel, calcium channel, trp channel, metal transport |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 4 |
| Total formula weight | 357405.55 |
| Authors | Zubcevic, L.,Hsu, A.L.,Borgnia, M.J.,Lee, S.-Y. (deposition date: 2019-04-22, release date: 2019-05-29, Last modification date: 2024-03-20) |
| Primary citation | Zubcevic, L.,Hsu, A.L.,Borgnia, M.J.,Lee, S.Y. Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes. Elife, 8:-, 2019 Cited by 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 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. PubMed: 31090543DOI: 10.7554/eLife.45779 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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