Crystal structure of the β2 adrenergic receptor–Gs protein complex
Open accessAbstract
G protein-coupled receptors (GPCRs) are responsible for the majority of cellular responses to hormones and neurotransmitters as well as the senses of sight, olfaction and taste. The paradigm of GPCR signalling is the activation of a heterotrimeric GTP binding protein (G protein) by an agonist-occupied receptor. The β(2) adrenergic receptor (β(2)AR) activation of Gs, the stimulatory G protein for adenylyl cyclase, has long been a model system for GPCR signalling. Here we present the crystal structure of the active state ternary complex composed of agonist-occupied monomeric β(2)AR and nucleotide-free Gs heterotrimer. The principal interactions between the β(2)AR and Gs involve the amino- and carboxy-terminal α-helices of Gs, with conformational changes propagating to the nucleotide-binding pocket. The largest conformational changes in the β(2)AR include a 14 Å outward movement at the cytoplasmic end of transmembrane segment 6 (TM6) and an α-helical extension of the cytoplasmic end of TM5. The most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain. This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR.
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Ligand binding to beta-adrenergic receptors results in a conformational change that activates Gs protein complexes.
“For example, ligand binding to beta-adrenergic receptors (ARs) results in a conformational change that activates Gs protein complexes [78].”
From G protein-coupled receptors function as cell membrane receptors for the steroid hormone 20-hydroxyecdysone (2020) · cites this paper as [78]
In classical GPCR signaling pathways, ligands bind to cell surface transmembrane receptors, such as β2 ARs, and cause conformational changes in their transmembrane and intracellular domains.
“In classical GPCR signaling pathways, ligands bind to cell surface transmembrane receptors, such as the β2 ARs, and cause conformational changes in their transmembrane and intracellular domains [48].”
From G-protein-coupled receptor participates in 20-hydroxyecdysone signaling on the plasma membrane (2014) · cites this paper as [48]
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- Authors
- Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., Mathiesen, J. M., Shah, S. T. A., Lyons, J. A., Caffrey, M., Gellman, S. H., Steyaert, J., Skiniotis, G., Weis, W. I., Sunahara, R. K., & Kobilka, B. K.
- Affiliations
- University of Copenhagen (DK)
- University of Michigan (US)
- Stanford Medicine (US)
- University of Wisconsin–Madison (US)
- Vrije Universiteit Brussel (BE)
- Trinity College Dublin (IE)
- Corresponding author
- Sunahara, Roger K.
- Kobilka, Brian K.
- ORCID
- Venue
- Nature
- Published
- 2011-07-19
- Volume
- 477
- Issue
- 7366
- Pages
- 549-555
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3184188
- OpenAlex
- W2167857702
- Cited by
- 3,009
- References
- 48
- Citations by year
- 2026: 93 · 2025: 145 · 2024: 159 · 2023: 147 · 2022: 161 · 2021: 168 · 2020: 177 · 2019: 195 · 2018: 212 · 2017: 234 · 2016: 238 · 2015: 258 · 2014: 255 · 2013: 301 · 2012: 202
- FWCI
- 107.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Scopus (Elsevier) (submittedVersion)
- VUBIR (Vrije Universiteit Brussel) (submittedVersion)
- Funders
- Sundhed og Sygdom, Det Frie Forskningsråd
- Science Foundation Ireland (07/IN.1/B1836)
- Fonds Wetenschappelijk Onderzoek
- Lundbeckfonden (R19-2008-2113, R37-2009-3457)
- Danmarks Frie Forskningsfond
- Vlaamse regering
- H. Lundbeck A/S
- National Institutes of Health (GM56169, GM75915)
- National Institute of General Medical Sciences (R01GM075915, U54GM094599, GM083118, GM 56169, P01GM075913, P01 GM75913, R01GM083118, P50GM073210, T32GM008270, GM75915, R01GM056169, R01GM068603)
- National Institute of Diabetes and Digestive and Kidney Diseases (P60DK020572, P60 DK 20572)
- National Institute of Neurological Disorders and Stroke (NS-028471, R01NS028471, R37NS028471)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- beta2-adrenergic receptor, Gs protein, G protein-coupled receptors, G protein-coupled receptor signaling, adenylate cyclase, GPCR crystal structures, protein dynamics
- MeSH terms
- Animals, Cattle, Crystallization, Enzyme Activation, Models, Molecular, Protein Binding, Receptors, Adrenergic, beta-2, Crystallography, X-Ray, GTP-Binding Protein alpha Subunits, Gs, Catalytic Domain, Multiprotein Complexes, Rats, Adrenergic beta-2 Receptor Agonists
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