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Biochim Biophys Acta. 2007 Aug;1771(8):915-25. Epub 2007 Jan 18.

Peroxisome proliferator-activated receptor structures: ligand specificity, molecular switch and interactions with regulators.

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  • 1Swiss Institute of Bioinformatics (SIB), Quartier Sorge, Batiment Genopode, CH-1015 Lausanne, Switzerland.

Abstract

Peroxisome proliferator-activated receptors (PPARs) compose a family of nuclear receptors that mediate the effects of lipidic ligands at the transcriptional level. In this review, we highlight advances in the understanding of the PPAR ligand binding domain (LBD) structure at the atomic level. The overall structure of PPARs LBD is described, and important protein ligand interactions are presented. Structure-activity relationships between isotypes structures and ligand specificity are addressed. It is shown that the numerous experimental three-dimensional structures available, together with in silico simulations, help understanding the role played by the activating function-2 (AF-2) in PPARs activation and its underlying molecular mechanism. The relation between the PPARs constitutive activity and the intrinsic stability of the active conformation is discussed. Finally, the interactions of PPARs LBD with co-activators or co-repressors, as well as with the retinoid X receptor (RXR) are described and considered in relation to PPARs activation.

PMID:
17317294
[PubMed - indexed for MEDLINE]
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