PDBsum entry 2vv4

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Receptor PDB id
Protein chain
254 a.a. *
Waters ×144
* Residue conservation analysis
PDB id:
Name: Receptor
Title: Hppargamma ligand binding domain in complex with 6-oxoote
Structure: Peroxisome proliferator-activated receptor gamma. Chain: a. Fragment: ligand binding domain, residues 202-475. Synonym: ppar gamma, nuclear receptor subfamily 1 group c member 3. Engineered: yes. Other_details: 6-oxoote. Peroxisome proliferator-activated receptor gamma. Chain: b.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: rosetta.
2.35Å     R-factor:   0.226     R-free:   0.252
Authors: T.Itoh,L.Fairall,J.W.R.Schwabe
Key ref: T.Itoh et al. (2008). Structural basis for the activation of PPARgamma by oxidized fatty acids. Nat Struct Mol Biol, 15, 924-931. PubMed id: 19172745
02-Jun-08     Release date:   19-Aug-08    
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Protein chains
Pfam   ArchSchema ?
P37231  (PPARG_HUMAN) -  Peroxisome proliferator-activated receptor gamma
505 a.a.
254 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     steroid hormone mediated signaling pathway   2 terms 
  Biochemical function     DNA binding     4 terms  


Nat Struct Mol Biol 15:924-931 (2008)
PubMed id: 19172745  
Structural basis for the activation of PPARgamma by oxidized fatty acids.
T.Itoh, L.Fairall, K.Amin, Y.Inaba, A.Szanto, B.L.Balint, L.Nagy, K.Yamamoto, J.W.Schwabe.
The nuclear receptor peroxisome proliferator-activated receptor-gamma (PPARgamma) has important roles in adipogenesis and immune response as well as roles in both lipid and carbohydrate metabolism. Although synthetic agonists for PPARgamma are widely used as insulin sensitizers, the identity of the natural ligand(s) for PPARgamma is still not clear. Suggested natural ligands include 15-deoxy-delta12,14-prostaglandin J2 and oxidized fatty acids such as 9-HODE and 13-HODE. Crystal structures of PPARgamma have revealed the mode of recognition for synthetic compounds. Here we report structures of PPARgamma bound to oxidized fatty acids that are likely to be natural ligands for this receptor. These structures reveal that the receptor can (i) simultaneously bind two fatty acids and (ii) couple covalently with conjugated oxo fatty acids. Thermal stability and gene expression analyses suggest that such covalent ligands are particularly effective activators of PPARgamma and thus may serve as potent and biologically relevant ligands.