TY - JOUR
T1 - Peroxisome proliferator-activated receptors (PPARs) have multiple binding points that accommodate ligands in various conformations
T2 - Phenylpropanoic acid-type PPAR ligands bind to PPAR in different conformations, depending on the subtype
AU - Kuwabara, Naoyuki
AU - Oyama, Takuji
AU - Tomioka, Daisuke
AU - Ohashi, Masao
AU - Yanagisawa, Junn
AU - Shimizu, Toshiyuki
AU - Miyachi, Hiroyuki
PY - 2012/1/26
Y1 - 2012/1/26
N2 - 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.
AB - 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.
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U2 - 10.1021/jm2014293
DO - 10.1021/jm2014293
M3 - Article
C2 - 22185225
AN - SCOPUS:84863393296
VL - 55
SP - 893
EP - 902
JO - Journal of Medicinal Chemistry
JF - Journal of Medicinal Chemistry
SN - 0022-2623
IS - 2
ER -