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

Naoyuki Kuwabara, Takuji Oyama, Daisuke Tomioka, Masao Ohashi, Junn Yanagisawa, Toshiyuki Shimizu, Hiroyuki Miyachi

Research output: Contribution to journalArticle

26 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)893-902
Number of pages10
JournalJournal of Medicinal Chemistry
Volume55
Issue number2
DOIs
Publication statusPublished - Jan 26 2012

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Peroxisome Proliferator-Activated Receptors
Ligands
Acids
Transcription Factors

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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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. / Kuwabara, Naoyuki; Oyama, Takuji; Tomioka, Daisuke; Ohashi, Masao; Yanagisawa, Junn; Shimizu, Toshiyuki; Miyachi, Hiroyuki.

In: Journal of Medicinal Chemistry, Vol. 55, No. 2, 26.01.2012, p. 893-902.

Research output: Contribution to journalArticle

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