6oo4

Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in amphipol resolved to 3.3 ACryo-EM structure of the C2-symmetric TRPV2/RTx complex in amphipol resolved to 3.3 A

6oo4, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Structural highlights 6oo4 is a 4 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G1SNM3_RABIT Publication Abstract from PubMed 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. Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes.,Zubcevic L, Hsu AL, Borgnia MJ, Lee SY Elife. 2019 May 15;8. pii: 45779. doi: 10.7554/eLife.45779. PMID:31090543 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels 3D structures