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- W2910817182 endingPage "478.e11" @default.
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- W2910817182 abstract "Biased G protein-coupled receptor (GPCR) agonists preferentially activate pathways mediated by G proteins or β-arrestins. Here, we use double electron-electron resonance spectroscopy to probe the changes that ligands induce in the conformational distribution of the angiotensin II type I receptor. Monitoring distances between 10 pairs of nitroxide labels distributed across the intracellular regions enabled mapping of four underlying sets of conformations. Ligands from different functional classes have distinct, characteristic effects on the conformational heterogeneity of the receptor. Compared to angiotensin II, the endogenous agonist, agonists with enhanced Gq coupling more strongly stabilize an open conformation with an accessible transducer-binding site. β-arrestin-biased agonists deficient in Gq coupling do not stabilize this open conformation but instead favor two more occluded conformations. These data suggest a structural mechanism for biased ligand action at the angiotensin receptor that can be exploited to rationally design GPCR-targeting drugs with greater specificity of action." @default.
- W2910817182 created "2019-01-25" @default.
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- W2910817182 date "2019-01-01" @default.
- W2910817182 modified "2023-10-16" @default.
- W2910817182 title "Angiotensin Analogs with Divergent Bias Stabilize Distinct Receptor Conformations" @default.
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- W2910817182 doi "https://doi.org/10.1016/j.cell.2018.12.005" @default.
- W2910817182 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6475118" @default.
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