› 2pnn

X-ray diffraction
2.7Å resolution

Crystal Structure of the Ankyrin Repeat Domain of Trpv1

Released:
DOI: 10.2210/pdb2pnn/pdb
PDB entry 2pnn coloured by chain, front view.
PDB entry 2pnn coloured by chain, side view.
PDB entry 2pnn coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity.
Lishko PV, Procko E, Jin X, Phelps CB, Gaudet R
Neuron 54 905-18 (2007)
PMID: 17582331

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128683 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transient receptor potential cation channel subfamily V member 1 Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 30.44 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O35433 (Residues: 101-364; Coverage: 32%)
Gene names: Trpv1, Vr1, Vr1l
Sequence domains: Ankyrin repeat
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

1 bound ligand:
Ligand ATP 1 x ATP
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R3
Unit cell:
a: 99.469Å b: 99.469Å c: 106.729Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.199 0.248
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

85 review citations

TRP channels and pain.
Julius D. (2013)
84 more

21 mentions without citation

Molecular mechanism of TRP channels.
Zheng J. (2013)
20 more