期刊
STRUCTURE
卷 28, 期 5, 页码 555-+出版社
CELL PRESS
DOI: 10.1016/j.str.2020.03.007
关键词
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资金
- National Key R&D Program of China [2018YFA0507103]
- National Major Scientific and Technological Special Project [2018ZX09711003-003-004, 2019ZX09721001-004-007]
- National Natural Science Foundation of China [31870719, 11774011]
- Shenzhen San-Ming Project [SZSM201809085]
- Shenzhen STIC [JCYJ20170307-110657570, JCYC20170817-110434640]
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-1 R. We reconstructed the IGF-1 R/insulin complex at 4.7 angstrom and the IGF-1 R/IGF-1 complex at 7.7 angstrom. Our structures reveal that only one insulin or one IGF-1 molecule binds to and activates the full-length human IGF-1R receptor.
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