› 6oo7

Electron Microscopy
3.8Å resolution

Cryo-EM structure of the C2-symmetric TRPV2/RTx complex in nanodiscs

Released:
DOI: 10.2210/pdb6oo7/pdb
PDB entry 6oo7 coloured by chain, front view.
PDB entry 6oo7 coloured by chain, side view.
PDB entry 6oo7 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes.
Zubcevic L, Hsu AL, Borgnia MJ, Lee SY
OpenAccess logo Elife 8 (2019)
PMID: 31090543
Related structures: EMD-20148

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ion transport domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 786 amino acids
Theoretical weight: 88.72 KDa
Source organism: Oryctolagus cuniculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: G1SNM3 (Residues: 56-817; Coverage: 93%)
Gene name: TRPV2
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand 6EU 4 x 6EU
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.8Å
Relevant EMDB volumes: EMD-20148
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

The role of π-helices in TRP channel gating.
Zubcevic et al. (2019)
6 more

9 mentions without citation

Structural insights into the gating mechanisms of TRPV channels.
Pumroy et al. (2020)
8 more