› 6d7l

Electron Microscopy
4Å resolution

Cytoplasmic domain of TRPC3

Released:
DOI: 10.2210/pdb6d7l/pdb
PDB entry 6d7l coloured by chain, front view.
PDB entry 6d7l coloured by chain, side view.
PDB entry 6d7l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating.
Sierra-Valdez F, Azumaya CM, Romero LO, Nakagawa T, Cordero-Morales JF
J Biol Chem 293 16102-16114 (2018)
PMID: 30139744
Related structures: EMD-7823

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-171729 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Short transient receptor potential channel 3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 853 amino acids
Theoretical weight: 97.87 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q13507 (Residues: 73-921; Coverage: 92%)
Gene names: TRP3, TRPC3
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4Å
Relevant EMDB volumes: EMD-7823
Expression system: Spodoptera frugiperda

Quick links

Citations

11 review citations

TRPC channels: Structure, function, regulation and recent advances in small molecular probes.
Wang et al. (2020)
10 more

1 mention without citation

Structure-function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating.
Sierra-Valdez et al. (2018)