2F4B

Crystal structure of the ligand binding domain of human PPAR-gamma in complex with an agonist

Summary for 2F4B

• Entry DOI: 10.2210/pdb2f4b/pdb
• Descriptor: Peroxisome proliferator-activated receptor gamma, (5-{3-[(6-BENZOYL-1-PROPYL-2-NAPHTHYL)OXY]PROPOXY}-1H-INDOL-1-YL)ACETIC ACID (3 entities in total)
• Functional Keywords: ppar, transcription activator
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P37231
• Total number of polymer chains: 2
• Total formula weight: 62515.65

Authors

Lu, I.L.,Peng, Y.H.,Mahindroo, N.,Hsieh, H.P.,Wu, S.Y. (deposition date: 2005-11-23, release date: 2006-02-14, Last modification date: 2024-03-13)

Primary citation

Mahindroo, N.,Wang, C.C.,Liao, C.C.,Huang, C.F.,Lu, I.L.,Lien, T.W.,Peng, Y.H.,Huang, W.J.,Lin, Y.T.,Hsu, M.C.,Lin, C.H.,Tsai, C.H.,Hsu, J.T.,Chen, X.,Lyu, P.C.,Chao, Y.S.,Wu, S.Y.,Hsieh, H.P.
Indol-1-yl Acetic Acids as Peroxisome Proliferator-Activated Receptor Agonists: Design, Synthesis, Structural Biology, and Molecular Docking Studies
J.Med.Chem., 49:1212-1216, 2006

PubMed Abstract: A series of novel indole-based PPAR agonists is described leading to discovery of 10k, a highly potent PPAR pan-agonist. The structural biology and molecular docking studies revealed that the distances between the acidic group and the linker, when a ligand was complexed with PPARgamma protein, were important for the potent activity. The hydrophobic tail part of 10k makes intensive hydrophobic interaction with the PPARgamma protein resulting in potent activity.

PubMed: 16451087
DOI: 10.1021/jm0510373

Experimental method

X-RAY DIFFRACTION (2.07 Å)