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- W4200459747 abstract "β-arrestins (βarrs) play multifaceted roles in the function of G protein-coupled receptors (GPCRs). βarrs typically interact with phosphorylated C-terminal tail (C tail) and transmembrane core (TM core) of GPCRs. However, the effects of the C tail- and TM core-mediated interactions on the conformational activation of βarrs have remained elusive. Here, we show the conformational changes for βarr activation upon the C tail- and TM core-mediated interactions with a prototypical GPCR by nuclear magnetic resonance (NMR) spectroscopy. Our NMR analyses demonstrated that while the C tail-mediated interaction alone induces partial activation, in which βarr exists in equilibrium between basal and activated conformations, the TM core- and the C tail-mediated interactions together completely shift the equilibrium toward the activated conformation. The conformation-selective antibody, Fab30, promotes partially activated βarr into the activated-like conformation. This plasticity of βarr conformation in complex with GPCRs engaged in different binding modes may explain the multifunctionality of βarrs." @default.
- W4200459747 created "2021-12-31" @default.
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- W4200459747 date "2021-12-09" @default.
- W4200459747 modified "2023-10-15" @default.
- W4200459747 title "Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR" @default.
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- W4200459747 doi "https://doi.org/10.1038/s41467-021-27482-3" @default.
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