Structural insight into PPARgamma activation through covalent modification with endogenous fatty acids.

@article{Waku2009StructuralII,
  title={Structural insight into PPARgamma activation through covalent modification with endogenous fatty acids.},
  author={Tsuyoshi Waku and Takuma Shiraki and Takuji Oyama and Yoshito Fujimoto and Kanako Maebara and Narutoshi Kamiya and Hisato Jingami and Kosuke Morikawa},
  journal={Journal of molecular biology},
  year={2009},
  volume={385 1},
  pages={188-99}
}
Peroxisome proliferator-activated receptor (PPAR) gamma is a nuclear receptor that regulates lipid homeostasis, and several fatty acid metabolites have been identified as PPARgamma ligands. Here, we present four crystal structures of the PPARgamma ligand binding domain (LBD) covalently bound to endogenous fatty acids via a unique cysteine, which is reportedly critical for receptor activation. The structure analyses of the LBD complexed with 15-deoxy-Delta(12,14)-prostaglandin J(2) (15d-PGJ(2… CONTINUE READING

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