Evidence map›Paper›PMID 21228869›Full record

ArticleNature2011

Structure of a nanobody-stabilized active state of the β(2) adrenoceptor.

Søren G F Rasmussen, Hee-Jung Choi, Juan Jose Fung, Els Pardon, Paola Casarosa, Pil Seok Chae, Brian T Devree, Daniel M Rosenbaum, Foon Sun Thian, Tong Sun Kobilka and 8 more

Abstract read
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 870 papers.

0numbers the graph read from it
0cells of the map it votes in
870citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

870 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Factors modulating the assembly of human βNature structural & molecular biology · 2026
    Article
  7. Article
  8. Article
  9. Nano-GAngewandte Chemie (International ed. in English) · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

810 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors.

Søren G F RasmussenDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, 279 Campus Drive, Stanford, California 94305, USA.
Hee-Jung Choi
Juan Jose Fung
Els Pardon
Paola Casarosa
Pil Seok Chae
Brian T Devree
Daniel M Rosenbaum
Foon Sun Thian
Tong Sun Kobilka
Andreas Schnapp
Ingo Konetzki
Roger K Sunahara
Samuel H Gellman
Alexander Pautsch
Jan Steyaert
William I Weis
Brian K Kobilka

Funding

PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
Structure and dynamics of G protein coupled receptor-G protein complexesR01GM083118 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOBILKA, BRIAN K, SKINIOTIS, GEORGIOS · 2008 to 2023
$8.3M
THE MECHANISM OF BETA2 ADRENOCEPTOR ACTIVATIONR01NS028471 · NINDS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 1990 to 2021
$6.7M
CATENINS, CADHERINS AND THEIR INTERACTIONSR01GM056169 · NIGMS · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 1997 to 2012
$5.0M
Synthesis/evaluation of novel surfactants for membrane protein structural biologyP01GM075913 · NIGMS · UNIVERSITY OF CHICAGO · PI LAIBLE, PHILIP D · 2005 to 2009
$4.2M
Beta2 Adrenoceptor Structure and Mechanism of ActivationR37NS028471 · NINDS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 2005 to 2011
$3.9M
Structure and mechanism of beta2-adrenergic receptorR01GM068603 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUNAHARA, ROGER K · 2003 to 2008
$1.6M
NIDDK NIH HHS P60DK-20572NIGMS NIH HHS GM083118NIGMS NIH HHS GM56169NIGMS NIH HHS P01 GM75913NIGMS NIH HHS R01 GM056169NIGMS NIH HHS R01 GM068603NIGMS NIH HHS R01 GM083118NINDS NIH HHS NS028471NINDS NIH HHS R01 NS028471NINDS NIH HHS R37 NS028471
6 · The paper itself

Abstract

G protein coupled receptors (GPCRs) exhibit a spectrum of functional behaviours in response to natural and synthetic ligands. Recent crystal structures provide insights into inactive states of several GPCRs. Efforts to obtain an agonist-bound active-state GPCR structure have proven difficult due to the inherent instability of this state in the absence of a G protein. We generated a camelid antibody fragment (nanobody) to the human β(2) adrenergic receptor (β(2)AR) that exhibits G protein-like behaviour, and obtained an agonist-bound, active-state crystal structure of the receptor-nanobody complex. Comparison with the inactive β(2)AR structure reveals subtle changes in the binding pocket; however, these small changes are associated with an 11 Å outward movement of the cytoplasmic end of transmembrane segment 6, and rearrangements of transmembrane segments 5 and 7 that are remarkably similar to those observed in opsin, an active form of rhodopsin. This structure provides insights into the process of agonist binding and activation.

Indexed as

Adrenergic beta-2 Receptor AgonistsAnimalsBinding SitesCamelids, New WorldCrystallography, X-RayDrug Inverse AgonismHumansImmunoglobulin FragmentsLigandsModels, MolecularMovementNanostructuresOpsinsPropanolaminesProtein ConformationProtein StabilityAdrenergic beta-2 Receptor Agonistscarazololgene 5 protein, Enterobacteria phage T4Immunoglobulin FragmentsLigandsOpsinsPropanolaminesReceptors, Adrenergic, beta-2Viral Proteins

Identifiers

PMID21228869
PMCPMC3058308

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.