Evidence map›Paper›PMID 26258638›Full record

ArticleNature structural & molecular biology2015

Probing Gαi1 protein activation at single-amino acid resolution.

Dawei Sun, Tilman Flock, Xavier Deupi, Shoji Maeda, Milos Matkovic, Sandro Mendieta, Daniel Mayer, Roger Dawson, Gebhard F X Schertler, M Madan Babu and 1 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Review
  2. Ligand-dependent G protein dynamics underlying opioid efficacy.Nature structural & molecular biology · 2026
    Article
  3. Article
  4. Article
  5. Ligand-dependent G protein dynamics underlying opioid signaling efficacy.bioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Characterisation of aEndocrine oncology (Bristol, England) · 2025
    Article
  8. Agonist efficacy at the βFrontiers in pharmacology · 2025
    Article
  9. Structure of endothelin ETCommunications biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. G Protein Activation Occurs via a Largely Universal Mechanism.The journal of physical chemistry. B · 2024
    Article
  14. Article
  15. Article
  16. Observational
  17. Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021
    Review
  18. Review
  19. Article
  20. Article
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

11 authors.

Dawei SunLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Tilman Flock *Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
Xavier Deupi *Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Shoji MaedaLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Milos MatkovicLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Sandro MendietaLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Daniel MayerLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Roger DawsonF. Hoffmann-La Roche AG, Pharma Research & Early Development, Discovery Technologies, Basel, Switzerland.
Gebhard F X SchertlerLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
M Madan BabuMedical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
Dmitry B VeprintsevLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.

Funding

Medical Research Council MC_U105185859
6 · The paper itself

Abstract

We present comprehensive maps at single-amino acid resolution of the residues stabilizing the human Gαi1 subunit in nucleotide- and receptor-bound states. We generated these maps by measuring the effects of alanine mutations on the stability of Gαi1 and the rhodopsin-Gαi1 complex. We identified stabilization clusters in the GTPase and helical domains responsible for structural integrity and the conformational changes associated with activation. In activation cluster I, helices α1 and α5 pack against strands β1-β3 to stabilize the nucleotide-bound states. In the receptor-bound state, these interactions are replaced by interactions between α5 and strands β4-β6. Key residues in this cluster are Y320, which is crucial for the stabilization of the receptor-bound state, and F336, which stabilizes nucleotide-bound states. Destabilization of helix α1, caused by rearrangement of this activation cluster, leads to the weakening of the interdomain interface and release of GDP.

Indexed as

Amino AcidsDNADNA Mutational AnalysisGTP-Binding Protein alpha SubunitsHumansModels, MolecularProtein BindingProtein ConformationProtein StabilityRhodopsinAmino AcidsDNAGTP-Binding Protein alpha SubunitsRhodopsin

Identifiers

PMID26258638
PMCPMC4876908

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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.