Article: article from journal or magazin.
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Peroxisome proliferator-activated receptor structures: ligand specificity, molecular switch and interactions with regulators.
Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Review Publication Status: ppublish
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.
Animals, Humans, Ligands, Models, Molecular, PPAR alpha/chemistry, PPAR alpha/physiology, Peroxisome Proliferator-Activated Receptors/chemistry, Peroxisome Proliferator-Activated Receptors/genetics, Protein Conformation, Substrate Specificity
Web of science
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