The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The Dynamic Process of β2-Adrenergic Receptor Activation
Open accessAbstract
G protein-coupled receptors (GPCRs) can modulate diverse signaling pathways, often in a ligand-specific manner. The full range of functionally relevant GPCR conformations is poorly understood. Here we use NMR spectroscopy to characterize the conformational dynamics of the transmembrane core of the β2-adrenergic receptor (β2AR), a prototypical GPCR. We labeled β2AR with 13CH3ε-methionine and obtained HSQC spectra of unliganded receptor as well as receptor bound to an inverse agonist, an agonist, and a G protein-mimetic nanobody. These studies provide evidence for conformational states not observed in crystal structures, as well as substantial conformational heterogeneity in agonist- and inverse-agonist-bound preparations. They also show that for β2AR, unlike rhodopsin, an agonist alone does not stabilize a fully active conformation, suggesting that the conformational link between the agonist-binding pocket and the G-protein-coupling surface is not rigid. The observed heterogeneity may be important for β2AR’s ability to engage multiple signaling and regulatory proteins.
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Crystal structure of the β2 adrenergic receptor–Gs protein complex
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Self-citationDynamic personalities of proteins
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The structure and function of G-protein-coupled receptors
Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K. (2009) · Nature · doi:10.1038/nature08144 · Cited by 2,534
Self-citationCrystal structure of metarhodopsin II
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Self-citationA G protein-coupled receptor at work: the rhodopsin model
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Roth, B. L. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.040 · Cited by 1,742
The Molecular Basis of G Protein–Coupled Receptor Activation
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Self-citationA genetically encoded fluorescent sensor for rapid and specific in vivo detection of norepinephrine
Feng, J., Zhang, C., Lischinsky, J. E., Jing, M., Zhou, J., Wang, H., Zhang, Y., Dong, A., Wu, Z., Wu, H., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.02.037 · Cited by 545
Muscarinic acetylcholine receptors: novel opportunities for drug development
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Self-citationStaus, D. P., Strachan, R. T., Manglik, A., Pani, B., Kahsai, A. W., Kim, T. H., Wingler, L. M., Ahn, S., Chatterjee, A., Masoudi, A., et al. (2016) · Nature · doi:10.1038/nature18636 · Cited by 330
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Metadata
- Authors
- Nygaard, R., Zou, Y., Dror, R. O., Mildorf, T. J., Arlow, D. H., Manglik, A., Pan, A. C., Liu, C. W., Fung, J. J., Bokoch, M. P., Thian, F. S., Kobilka, T. S., Shaw, D. E., Mueller, L., Prosser, R. S., & Kobilka, B. K.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 152
- Issue
- 3
- Pages
- 532-542
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2162109316
- Cited by
- 796
- References
- 8
- FWCI
- 43.98
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Nygaard, R., Zou, Y., Dror, R. O., Mildorf, T. J., Arlow, D. H., Manglik, A., Pan, A. C., Liu, C. W., Fung, J. J., Bokoch, M. P., Thian, F. S., Kobilka, T. S., Shaw, D. E., Mueller, L., Prosser, R. S., & Kobilka, B. K. (2013). The Dynamic Process of β2-Adrenergic Receptor Activation. Cell. https://doi.org/10.1016/j.cell.2013.01.008
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