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Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR
Open accessAbstract
Choosing a Path: The β 2 -adrenergic receptor (β 2 AR) is a G protein–coupled receptor that recognizes diverse ligands to trigger signaling in the cell. Besides binding G proteins, activated β 2 AR can be phosphorylated and bind arrestin, which redirects signaling to other pathways. Some β 2 AR ligands are “biased” in that they differentially activate G protein or arrestin signaling. Liu et al. (p. 1106 , published online 19 January; see the Perspective by Sprang and Chief Elk ) used 19 F-NMR spectroscopy to examine conformational changes associated with a range of ligands and discovered that biased ligands caused differential shifts in equilibrium between two conformational states—the G protein binding state and the arrestin binding state—and thus provide a basis for rational design of pharmacological ligands.
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Crystal structure of the β2 adrenergic receptor–Gs protein complex
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Crystal structure of opsin in its G-protein-interacting conformation
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The role of kinetic context in apparent biased agonism at GPCRs
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Rational design of 19F NMR labelling sites to probe protein structure and interactions
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Metadata
- Authors
- Liu, J. J., Horst, R., Katritch, V., Stevens, R. C., & Wüthrich, K.
- Venue
- Science
- Published
- 2012-03-02
- Volume
- 335
- Issue
- 6072
- Pages
- 1106-1110
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2053549636
- Cited by
- 697
- References
- 3
- FWCI
- 26.95
- Type
- journal article
- Language
- en
- Open access
- green
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
