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On August 6, 2021, Beijing time, the team of Wang Mingwei/Yang Dehua and Xu Huaqiang/Zhao Lihua team of Shanghai Institute of Materia Medica, Chinese Academy of Sciences, and Jiang Hualiang/Cheng Xi’s team , published in the Proceedings of the National Academy of Sciences ( Proceedings of the National Academy of Sciences of the United States).
PTH2R is a member of the B1 G protein-coupled receptor family.
Previously, the team members mainly by analyzing the long-term PTH1R parathyroid hormone (Long-acting parathyroid hormone, LA -PTH) a three-dimensional structure of the complex was found outside of the extracellular domain PTH1R highly flexible 8 , but the specific PTH2R and PTH1R The molecular mechanism of sexual recognition of endogenous ligands is still unclear
Figure 1.
The study revealed that the PTH2R endogenous ligand TIP39 presents an amphipathic α-helix , with the carboxyl terminal interacting with the extracellular domain, and the amino terminal inserting into the receptor transmembrane domain
Figure 2.
Shanghai Institute of Materia Medica/Fudan University Chair Professor Wang Mingwei, Shanghai Institute of Materia Medica Researcher Yang Dehua, and Researcher Xu Huaqiang are the co-corresponding authors of the paper; Shanghai Institute of Materia Medica graduate students Wang Xi, Associate Researcher Cheng Xi and Associate Researcher Zhao Lihua are the co-first authors
Original link:
https:// Dobolyi, A.
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