› 2p4y

X-ray diffraction
2.25Å resolution

Crystal structure of human PPAR-gamma-ligand binding domain complexed with an indole-based modulator

Released:
DOI: 10.2210/pdb2p4y/pdb
PDB entry 2p4y coloured by chain, front view.
PDB entry 2p4y coloured by chain, side view.
PDB entry 2p4y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The differential interactions of peroxisome proliferator-activated receptor gamma ligands with Tyr473 is a physical basis for their unique biological activities.
Einstein M, Akiyama TE, Castriota GA, Wang CF, McKeever B, Mosley RT, Becker JW, Moller DE, Meinke PT, Wood HB, Berger JP
Mol Pharmacol 73 62-74 (2008)
PMID: 17940191

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisome proliferator-activated receptor gamma Chains: A, B
Molecule details ›
Chains: A, B
Length: 277 amino acids
Theoretical weight: 31.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P37231 (Residues: 231-505; Coverage: 55%)
Gene names: NR1C3, PPARG
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

2 bound ligands:
Ligand C03 2 x C03
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 92.148Å b: 59.859Å c: 118.287Å
α: 90° β: 103.76° γ: 90°
R-values:
R R work R free
0.232 0.232 0.274
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

MITF in melanoma: mechanisms behind its expression and activity.
Hartman et al. (2015)
7 more

9 mentions without citation

Review of the Structural and Dynamic Mechanisms of PPARĪ³ Partial Agonism.
Kroker et al. (2015)
8 more