› 2vv0

X-ray diffraction
2.55Å resolution

hPPARgamma Ligand binding domain in complex with DHA

Released:
DOI: 10.2210/pdb2vv0/pdb
PDB entry 2vv0 coloured by chain, front view.
PDB entry 2vv0 coloured by chain, side view.
PDB entry 2vv0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the activation of PPARgamma by oxidized fatty acids.
Itoh T, Fairall L, Amin K, Inaba Y, Szanto A, Balint BL, Nagy L, Yamamoto K, Schwabe JW
Nat Struct Mol Biol 15 924-31 (2008)
PMID: 19172745

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153368 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisome proliferator-activated receptor gamma Chains: A, B
Molecule details ›
Chains: A, B
Length: 276 amino acids
Theoretical weight: 31.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P37231 (Residues: 232-505; Coverage: 54%)
Gene names: NR1C3, PPARG
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:
Ligand HXA 2 x HXA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: C2
Unit cell:
a: 93.09Å b: 61.28Å c: 118.55Å
α: 90° β: 103.19° γ: 90°
R-values:
R R work R free
0.218 0.218 0.261
Expression system: Escherichia coli BL21

Quick links

Citations

82 review citations

PPARs are a unique set of fatty acid regulated transcription factors controlling both lipid metabolism and inflammation.
Varga et al. (2011)
81 more

7 mentions without citation

Small-Molecule Modulation of PPARs for the Treatment of Prevalent Vascular Retinal Diseases.
Dou et al. (2020)
6 more