Conformational adaptation of agonists to the human nuclear receptor RARγ

@article{Klaholz1998ConformationalAO,
  title={Conformational adaptation of agonists to the human nuclear receptor RARγ},
  author={B. Klaholz and J. Renaud and A. Mitschler and C. Zusi and P. Chambon and H. Gronemeyer and D. Moras},
  journal={Nature Structural Biology},
  year={1998},
  volume={5},
  pages={199-202}
}
The nuclear retinoid receptors RARs and RXRs are transcriptional regulators whose activity is mediated by their ligand-binding domain. The crystal structures of the unliganded human (apo) hRXRa ligand-binding domain and of the all-trans retinoic acid-liganded (holo) hRARγ ligand-binding domain have been described. We report the crystal structures of the hRARγ ligand-binding domain bound to either its other natural ligand 9-cis retinoic acid, or an RARγ-selective synthetic agonist (BMS961). The… Expand
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