Nature Communications (Sep 2020)

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

  • 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

DOI
https://doi.org/10.1038/s41467-020-18433-5
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 17

Abstract

Read online

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.