期刊
SCIENCE
卷 335, 期 6072, 页码 1106-1110出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1215802
关键词
-
资金
- NIH Roadmap Initiative [P50 GM073197]
- PSI [U54 GM094618]
Extracellular ligand binding to G protein-coupled receptors (GPCRs) modulates G protein and beta-arrestin signaling by changing the conformational states of the cytoplasmic region of the receptor. Using site-specific F-19-NMR (fluorine-19 nuclear magnetic resonance) labels in the beta(2)-adrenergic receptor (beta(2)AR) in complexes with various ligands, we observed that the cytoplasmic ends of helices VI and VII adopt two major conformational states. Changes in the NMR signals reveal that agonist binding primarily shifts the equilibrium toward the G protein-specific active state of helix VI. In contrast, beta-arrestin-biased ligands predominantly impact the conformational states of helix VII. The selective effects of different ligands on the conformational equilibria involving helices VI and VII provide insights into the long-range structural plasticity of beta(2)AR in partial and biased agonist signaling.
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