Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family.
Cronet, P., Petersen, J.F., Folmer, R., Blomberg, N., Sjoblom, K., Karlsson, U., Lindstedt, E.L., Bamberg, K.(2001) Structure 9: 699-701
- PubMed: 11587644 
- DOI: https://doi.org/10.1016/s0969-2126(01)00634-7
- Primary Citation of Related Structures:  
1I7G, 1I7I - PubMed Abstract: 
The peroxisome proliferator-activated receptors (PPAR) are ligand-activated transcription factors belonging to the nuclear receptor family. The roles of PPARalpha in fatty acid oxidation and PPARgamma in adipocyte differentiation and lipid storage have been characterized extensively. PPARs are activated by fatty acids and eicosanoids and are also targets for antidyslipidemic drugs, but the molecular interactions governing ligand selectivity for specific subtypes are unclear due to the lack of a PPARalpha ligand binding domain structure.
Organizational Affiliation: 
Department of Molecular Biology, AstraZeneca R&D Mölndal, S-431 83, Mölndal, Sweden.