Evidence map›Paper›PMID 34581758›Full record

ReviewBiochemical Society transactions2021

Structure determination of GPCRs: cryo-EM compared with X-ray crystallography.

Javier García-Nafría, Christopher G Tate

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.1field-weighted citation impact, top 2% of its field
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

68 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Nano-GAngewandte Chemie (International ed. in English) · 2026
    Article
  6. Advances in GPCR-Targeted PET Radiotracer Patents (2020-2025).Pharmaceuticals (Basel, Switzerland) · 2026
    Review
  7. Article
  8. A novel fusion tool to enable G protein-coupled receptor structure determination.Acta crystallographica. Section D, Structural biology · 2026
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  20. Article

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

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Javier García-NafríaInstitute for Biocomputation and Physics of Complex Systems (BIFI) and Laboratorio de Microscopías Avanzadas (LMA), University of Zaragoza, 50018 Zaragoza, Spain.
Christopher G TateMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, U.K.ORCID 0000-0002-2008-9183
MRC Laboratory of Molecular Biology · GBUniversidad de Zaragoza · ES

Funding

Medical Research Council MC_U105197215Medical Research Council U105197215
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are the largest single family of cell surface receptors encoded by the human genome and they play pivotal roles in co-ordinating cellular systems throughout the human body, making them ideal drug targets. Structural biology has played a key role in defining how receptors are activated and signal through G proteins and β-arrestins. The application of structure-based drug design (SBDD) is now yielding novel compounds targeting GPCRs. There is thus significant interest from both academia and the pharmaceutical industry in the structural biology of GPCRs as currently only about one quarter of human non-odorant receptors have had their structure determined. Initially, all the structures were determined by X-ray crystallography, but recent advances in electron cryo-microscopy (cryo-EM) now make GPCRs tractable targets for single-particle cryo-EM with comparable resolution to X-ray crystallography. So far this year, 78% of the 99 GPCR structures deposited in the PDB (Jan-Jul 2021) were determined by cryo-EM. Cryo-EM has also opened up new possibilities in GPCR structural biology, such as determining structures of GPCRs embedded in a lipid nanodisc and multiple GPCR conformations from a single preparation. However, X-ray crystallography still has a number of advantages, particularly in the speed of determining many structures of the same receptor bound to different ligands, an essential prerequisite for effective SBDD. We will discuss the relative merits of cryo-EM and X-ray crystallography for the structure determination of GPCRs and the future potential of both techniques.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayHumansLigandsProtein ConformationReceptors, G-Protein-CoupledLigandsReceptors, G-Protein-Coupledcryo-electron microscopycrystallographyG-protein-coupled receptors

Identifiers

PMID34581758
PMCPMC8589417
OpenAlexW3203752479

What OpenQuestion holds

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Registered trials

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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.