Brief Communication abstract

Nature Structural & Molecular Biology 15, 865 - 867 (2008)
Published online: 6 July 2008 | doi:10.1038/nsmb.1447

Molecular recognition of nitrated fatty acids by PPARbig gamma

Yong Li1,2, Jifeng Zhang3, Francisco J Schopfer4, Dariusz Martynowski1, Minerva T Garcia-Barrio5, Amanda Kovach2, Kelly Suino-Powell2, Paul R S Baker4, Bruce A Freeman4, Y Eugene Chen3 & H Eric Xu2

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Peroxisome proliferator activated receptor-gamma (PPARgamma) regulates metabolic homeostasis and adipocyte differentiation, and it is activated by oxidized and nitrated fatty acids. Here we report the crystal structure of the PPARgamma ligand binding domain bound to nitrated linoleic acid, a potent endogenous ligand of PPARgamma. Structural and functional studies of receptor-ligand interactions reveal the molecular basis of PPARgamma discrimination of various naturally occurring fatty acid derivatives.

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  1. Department of Pharmaceutical Sciences, Center for Pharmacogenetics, 709 Salk Hall, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
  2. Laboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan 49503, USA.
  3. Cardiovascular Center, Department of Internal Medicine, University of Michigan Medical Center, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109, USA.
  4. Department of Pharmacology and Chemical Biology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
  5. Cardiovascular Research Institute, Morehouse School of Medicine, 720 Westview Drive SW, Atlanta, Georgia 30310, USA.

Correspondence to: Yong Li1,2 e-mail: yol21@pitt.edu

Correspondence to: H Eric Xu2 e-mail: eric.xu@vai.org



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