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WANG Tao's Group | Study on visualization of ligand-bound ectodomain assembly in the full-length human IGF-1 receptor by Cryo-EM single-particle analysis
News/2020.04.16

April 2020, WANG Tao’s group published a research article on Structure, a leading journal for structural biology under Cell, reporting the cryo-EM structure of the ligand-bound ectodomain in the full-length human IGF-1R. In this research article named “Visualization of ligand-bound ectodomain assembly in the full-length human IGF-1 receptor by Cryo-EM single-particle analysis”, the group discussed how they reconstructed the IGF-1R/insulin complex at 4.7 Å and the IGF-1R/IGF-1 complex at 7.7 Å. The structures acquired by the study reveal that only one insulin or one IGF-1 molecule binds to and activates the full-length human IGF-1R receptor. (WANG Tao) To find out more about the article, please access: https://www.cell.com/structure/fulltext/S0969-2126(20)30079-4 https://www.pnas.org/content/early/2020/02/10/1911998117 Faculty of 1000:https://doi.org/10.3410/f.737364180.793571437 PNAS link:https://www.pnas.org/content/117/12/6292.long

April 2020, WANG Tao’s group published a research article on Structure, a leading journal for structural biology under Cell, reporting the cryo-EM structure of the ligand-bound ectodomain in the full-length human IGF-1R.

In this research article named “Visualization of ligand-bound ectodomain assembly in the full-length human IGF-1 receptor by Cryo-EM single-particle analysis”, the group discussed how they reconstructed the IGF-1R/insulin complex at 4.7 Å and the IGF-1R/IGF-1 complex at 7.7 Å. The structures acquired by the study reveal that only one insulin or one IGF-1 molecule binds to and activates the full-length human IGF-1R receptor.

汪涛.jpg

(WANG Tao)

To find out more about the article, please access:

https://www.cell.com/structure/fulltext/S0969-2126(20)30079-4

https://www.pnas.org/content/early/2020/02/10/1911998117

Faculty of 1000:https://doi.org/10.3410/f.737364180.793571437

PNAS link:https://www.pnas.org/content/117/12/6292.long