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. 2011 Aug 31;35(4):327–336. doi: 10.4093/dmj.2011.35.4.327

Fig. 1.

Fig. 1

Structure and molecular mechanism of action of peroxisome proliferator-activated receptor alpha (PPARα). (A) PPARα has four functional domains: the N-terminal ligand-independent transactivation domain (A/B domain); DNA binding domain (DBD or C domain), including an activation function-1 (AF-1); co-factor docking domain (D domain); and C-terminal E/F domain including a ligand binding domain (LBD) and an activation function-2 (AF-2). (B) The PPARα and retinoid X receptor-α (RXRα) heterodimer, which can recruit diverse coactivators and corepressors that modulate the transcriptional activity of PPARα, binds to PPAR-response elements (PPRE) to activate target gene transcription.