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Glucose-dependent insulinotropic polypeptide receptor (GIPR) belongs to the B1 type G protein-coupled receptor.
July 13, 2021, Shanghai Institute of Materia Medica, Chinese Academy of Mingwei / Yang Dehua team to join hands Xu Huaqiang team eLife delivered a presentation entitled "Structural insights into hormone recognition by the human glucose-dependent insulinotropic polypeptide receptor" research paper, first reported The high-resolution cryo-EM structure of human GIPR with GIP 1-42 and G s protein complexes revealed the molecular mechanism of ligand recognition and signal transduction of GIPR, thus completing three receptors closely related to blood glucose regulation.
In order to enhance the stability of the complex formed by GIPR and G s protein, the researchers used NanoBiT ligation technology 10 to introduce LgBiT and HiBiT (Peptide 86) on GIPR and G s protein respectively to increase the interaction between the proteins, and at the same time The receptor was subjected to single point mutations to improve the stability of the complex.
Figure 1.
Comparing the ligand recognition modes of glucagon receptor, glucagon-like peptide-1 receptor and GIPR, researchers found that these three receptors all have conserved amino acid residues that bind to the common region of the ligand.
Figure 2.
Fenghui Zhao, a doctoral student at the School of Pharmacy of Fudan University, Chao Zhang, a master student at the School of Life Sciences and Technology, ShanghaiTech University, Qingtong Zhou, a young researcher at the School of Basic Medicine, Fudan University, and Kaini Hang, a doctoral student at the iHuman Institute of ShanghaiTech University, are the co-first authors of the paper
Original link: https://elifesciences.
references:
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Song, G.
et al.
Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators.
Nature 546, 312-315 (2017).
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Sun, W.
et al.
A unique hormonal recognition feature of the human glucagon-like peptide-2 receptor.
Cell Res 30, 1098-1108 (2020).