DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe

DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe

Characterization of dynamic conformational changes in membrane protein complexes by NMR spectroscopy remains challenging. Here authors report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, which enabled the characterization of multiple conformational state...

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Autores principales: Qi Liu, Qing-tao He, Xiaoxuan Lyu, Fan Yang, Zhong-liang Zhu, Peng Xiao, Zhao Yang, Feng Zhang, Zhao-ya Yang, Xiao-yan Wang, Peng Sun, Qian-wen Wang, Chang-xiu Qu, Zheng Gong, Jing-yu Lin, Zhen Xu, Shao-le Song, Shen-ming Huang, Sheng-chao Guo, Ming-jie Han, Kong-kai Zhu, Xin Chen, Alem W. Kahsai, Kun-Hong Xiao, Wei Kong, Fa-hui Li, Ke Ruan, Zi-jian Li, Xiao Yu, Xiao-gang Niu, Chang-wen Jin, Jiangyun Wang, Jin-peng Sun
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Science
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Acceso en línea:https://doaj.org/article/9e525d39c3704658bb31c1f7b6676d76
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Sumario:Characterization of dynamic conformational changes in membrane protein complexes by NMR spectroscopy remains challenging. Here authors report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, which enabled the characterization of multiple conformational states of a phospho-β2 adrenergic receptor/β-arrestin-1 complex in response to different receptor ligands.

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