The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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 the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Fredriksson, R., Lagerström, M. C., Lundin, L.-G., & Schiöth, H. B. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.6.1256 · Cited by 2,941
Crystal structure of the human β2 adrenergic G-protein-coupled receptor
Rasmussen, S. G. F., Choi, H., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M. C., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., et al. (2007) · Nature · doi:10.1038/nature06325 · Cited by 1,935
Self-citationTransduction of Receptor Signals by ß-Arrestins
Lefkowitz, R. J., & Shenoy, S. K. (2005) · Science · doi:10.1126/science.1109237 · Cited by 1,729
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Rasmussen, S. G. F., Choi, H., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,709
Self-citationSolving structures of protein complexes by molecular replacement with Phaser
McCoy, A. (2006) · Acta Crystallographica Section D: Biological Crystallography · doi:10.1107/s0907444906045975 · Cited by 1,672
Léan, A. D., Stadel, J. M., & Lefkowitz, R. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79672-9 · Cited by 1,606
Research works printed but not linked: 1
- Chung, K. Y. et al. β2 adrenergic receptor-induced conformational changes in the heterotrimeric G protein Gs. Nature 10.1038/nature10488 (this issue) · DOI
Cited by
Sorted by citations
Items 1,001–1,004 of 1,004
García, M., González de Buitrago, J., Jiménez-Rosés, M., Pardo, L., Hinkle, P. M., & Moreno, J. C. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-3977 · Cited by 33
Ketamine Metabolite (2 R,6 R)-Hydroxynorketamine Interacts with μ and κ Opioid Receptors
Joseph, T. T., Bu, W., Lin, W., Zoubak, L., Yeliseev, A., Liu, R., Eckenhoff, R. G., & Brannigan, G. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00741 · Cited by 28
Nunes-Silva, S., Gangnard, S., Vidal, M., Vuchelen, A., Dechavanne, S., Chan, S., Pardon, E., Steyaert, J., Ramboarina, S., Chêne, A., et al. (2014) · Scientific Reports · doi:10.1038/srep07373 · Cited by 15
Self-citationNordquist, E. B., Zhao, M., Kumar, A., & MacKerell, A. D. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01189 · Cited by 15
Metadata
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
