1I7G

CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN FROM HUMAN PPAR-ALPHA IN COMPLEX WITH THE AGONIST AZ 242

Summary for 1I7G

• Entry DOI: 10.2210/pdb1i7g/pdb
• Related: 1I7I
• Descriptor: PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA, SODIUM ION, (2S)-2-ETHOXY-3-[4-(2-{4-[(METHYLSULFONYL)OXY]PHENYL}ETHOXY)PHENYL]PROPANOIC ACID, ... (5 entities in total)
• Functional Keywords: anti parallel helix sandwich, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q07869
• Total number of polymer chains: 1
• Total formula weight: 33630.86

Authors

Petersen, J.F.W.,Cronet, P.,Folmer, R.,Blomberg, N.,Sjoblom, K.,Karlsson, U.,Lindstedt, E.-L.,Bamberg, K. (deposition date: 2001-03-09, release date: 2002-03-09, Last modification date: 2023-08-09)

Primary citation

Cronet, P.,Petersen, J.F.,Folmer, R.,Blomberg, N.,Sjoblom, K.,Karlsson, U.,Lindstedt, E.L.,Bamberg, K.
Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family.
Structure, 9:699-706, 2001

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.

PubMed: 11587644
DOI: 10.1016/S0969-2126(01)00634-7

Experimental method

X-RAY DIFFRACTION (2.2 Å)