通过冷冻电镜单颗粒分析对全长人胰岛素样生长因子-1受体中配体结合胞外域组装体的可视化研究
Visualization of Ligand-Bound Ectodomain Assembly in the Full-Length Human IGF-1 Receptor by Cryo-EM Single-Particle Analysis.
作者信息
Zhang Xi, Yu Daqi, Sun Jingchuan, Wu Yujie, Gong Junyuan, Li Xuemei, Liu Li, Liu Shan, Liu Jianbo, Wu Yulan, Li Dongyang, Ma Yinping, Han Xu, Zhu Yanan, Wu Zhaolong, Wang Yihua, Ouyang Qi, Wang Tao
机构信息
School of Life Science and Technology, Harbin Institute of Technology, Harbin 150001, China; Department of Biology, Southern University of Science and Technology, Shenzhen 518055, China.
State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Beijing 100871, China.
出版信息
Structure. 2020 May 5;28(5):555-561.e4. doi: 10.1016/j.str.2020.03.007. Epub 2020 Apr 9.
Tyrosine kinase receptor of insulin-like growth factor 1 receptor (IGF-1R) and insulin receptor (IR) bind to hormones, such as insulin, IGF-1, and IGF-2, and transduces the signals across the cell membrane. However, the complete structure of the receptor and the signal transduction mechanism remains unclear. Here, we report the cryo-EM structure of the ligand-bound ectodomain in the full-length human IGF-1R. We reconstructed the IGF-1R/insulin complex at 4.7 Å and the IGF-1R/IGF-1 complex at 7.7 Å. Our structures reveal that only one insulin or one IGF-1 molecule binds to and activates the full-length human IGF-1R receptor.
胰岛素样生长因子1受体（IGF-1R）和胰岛素受体（IR）的酪氨酸激酶受体与胰岛素、IGF-1和IGF-2等激素结合，并将信号跨细胞膜传导。然而，受体的完整结构和信号转导机制仍不清楚。在此，我们报告了全长人IGF-1R中配体结合胞外域的冷冻电镜结构。我们分别以4.7 Å分辨率重构了IGF-1R/胰岛素复合物和以7.7 Å分辨率重构了IGF-1R/IGF-1复合物。我们的结构表明，只有一个胰岛素或一个IGF-1分子结合并激活全长人IGF-1R受体。
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