Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
oleh: Qing-Tao He, Peng Xiao, Shen-Ming Huang, Ying-Li Jia, Zhong-Liang Zhu, Jing-Yu Lin, Fan Yang, Xiao-Na Tao, Ru-Jia Zhao, Feng-Yuan Gao, Xiao-Gang Niu, Kun-Hong Xiao, Jiangyun Wang, Changwen Jin, Jin-Peng Sun, Xiao Yu
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2021-04-01 |
Deskripsi
The interaction between a GPCR, such as the vasopressin receptor-2 (V2R), and arrestin depends on the receptors’ phosphorylation pattern. Here authors use FRET and NMR to analyze the phosphorylation patterns of the V2R-arrestin complex and show that phospho-interactions are the key determinants of selective arrestin conformational states and correlated functions.