Cryo-EM structure of activated bile acids receptor TGR5 in complex with stimulatory G protein
Author:
Funder
National Natural Science Foundation of China
Shenzhen Science and Technology Innovation Committee
Publisher
Springer Science and Business Media LLC
Subject
Cancer Research,Genetics
Link
https://www.nature.com/articles/s41392-020-00262-z.pdf
Reference5 articles.
1. Maruyama, T. et al. Identification of membrane-type receptor for bile acids (M-BAR). Biochem. Biophys. Res. Commun.298, 714–719 (2002).
2. Deutschmann, K. et al. Bile acid receptors in the biliary tree: TGR5 in physiology and disease. Biochim. Biophys. Acta1864, 1319–1325 (2018).
3. Duan, H. et al. Design, synthesis, and antidiabetic activity of 4-phenoxynicotinamide and 4-phenoxypyrimidine-5-carboxamide derivatives as potent and orally efficacious TGR5 agonists. J. Med. Chem.55, 10475–10489 (2012).
4. Rasmussen, S. G. et al. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature477, 549–555 (2011).
5. Zhang, Y. et al. Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein. Nature546, 248–253 (2017).
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