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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adamantane / analogs & derivatives
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Adamantane / chemistry
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Binding Sites
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Crystallography, X-Ray
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Humans
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Hydrophobic and Hydrophilic Interactions
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Ligands
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Models, Molecular*
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Molecular Conformation
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PPAR alpha / agonists*
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PPAR alpha / chemistry
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PPAR delta / agonists*
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PPAR delta / chemistry
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PPAR gamma / agonists*
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PPAR gamma / chemistry
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Phenylpropionates / chemistry*
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Protein Conformation
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Recombinant Proteins / agonists
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Recombinant Proteins / chemistry
Substances
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Ligands
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PPAR alpha
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PPAR delta
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PPAR gamma
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Phenylpropionates
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Recombinant Proteins
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Adamantane
Associated data
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PDB/3VI8
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PDB/3VJH
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PDB/3VJI