3VI8
Human PPAR alpha ligand binding domain in complex with a synthetic agonist APHM13
Summary for 3VI8
| Entry DOI | 10.2210/pdb3vi8/pdb |
| Related | 2znn |
| Descriptor | Peroxisome proliferator-activated receptor alpha, (2S)-2-(4-methoxy-3-{[(pyren-1-ylcarbonyl)amino]methyl}benzyl)butanoic acid (3 entities in total) |
| Functional Keywords | nuclear receptor, protein-ligand complex, ppar, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q07869 |
| Total number of polymer chains | 1 |
| Total formula weight | 31321.59 |
| Authors | Oyama, T.,Miyachi, H.,Morikawa, K. (deposition date: 2011-09-25, release date: 2012-08-29, Last modification date: 2023-11-08) |
| Primary citation | Kuwabara, N.,Oyama, T.,Tomioka, D.,Ohashi, M.,Yanagisawa, J.,Shimizu, T.,Miyachi, H. Peroxisome proliferator-activated receptors (PPARs) have multiple binding points that accommodate ligands in various conformations: phenylpropanoic acid-type PPAR ligands bind to PPAR in different conformations, depending on the subtype J.Med.Chem., 55:893-902, 2012 Cited by PubMed Abstract: Human peroxisome proliferator-activated receptors (hPPARs) are ligand-dependent transcription factors that control various biological responses, and there are three subtypes: hPPARα, hPPARδ, and hPPARγ. We report here that α-substituted phenylpropanoic acid-type hPPAR agonists with similar structure bind to the hPPAR ligand binding domain (LBD) in different conformations, depending on the receptor subtype. These results might indicate that hPPAR ligand binding pockets have multiple binding points that can be utilized to accommodate structurally flexible hPPAR ligands. PubMed: 22185225DOI: 10.1021/jm2014293 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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