Evidence map›Paper›PMID 31727777›Full record

ArticleThe Journal of cell biology2020

Cryo-EM structure of the complete and ligand-saturated insulin receptor ectodomain.

Theresia Gutmann, Ingmar B Schäfer, Chetan Poojari, Beate Brankatschk, Ilpo Vattulainen, Mike Strauss, Ünal Coskun

Abstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing 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

67 citing papers in PubMed.

  1. Review
  2. Ligand regulation and function of preformed EGFR dimers.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  18. A λ-Dynamics Investigation of InsulinJournal of chemical information and modeling · 2024
    Article
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  20. Article

7 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

7 authors.

Theresia Gutmann *Paul Langerhans Institute Dresden of the Helmholtz Zentrum Munich at the University Hospital and Faculty of Medicine Carl Gustav Carus of Technische Universität Dresden, Dresden, Germany.
Ingmar B Schäfer *Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.
Chetan Poojari *Department of Physics, University of Helsinki, Helsinki, Finland.
Beate BrankatschkPaul Langerhans Institute Dresden of the Helmholtz Zentrum Munich at the University Hospital and Faculty of Medicine Carl Gustav Carus of Technische Universität Dresden, Dresden, Germany.
Ilpo VattulainenDepartment of Physics, University of Helsinki, Helsinki, Finland.
Mike StraussDepartment of Anatomy & Cell Biology, McGill University, Montreal, Quebec, Canada.
Ünal CoskunPaul Langerhans Institute Dresden of the Helmholtz Zentrum Munich at the University Hospital and Faculty of Medicine Carl Gustav Carus of Technische Universität Dresden, Dresden, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucose homeostasis and growth essentially depend on the hormone insulin engaging its receptor. Despite biochemical and structural advances, a fundamental contradiction has persisted in the current understanding of insulin ligand-receptor interactions. While biochemistry predicts two distinct insulin binding sites, 1 and 2, recent structural analyses have resolved only site 1. Using a combined approach of cryo-EM and atomistic molecular dynamics simulation, we present the structure of the entire dimeric insulin receptor ectodomain saturated with four insulin molecules. Complementing the previously described insulin-site 1 interaction, we present the first view of insulin bound to the discrete insulin receptor site 2. Insulin binding stabilizes the receptor ectodomain in a T-shaped conformation wherein the membrane-proximal domains converge and contact each other. These findings expand the current models of insulin binding to its receptor and of its regulation. In summary, we provide the structural basis for a comprehensive description of ligand-receptor interactions that ultimately will inform new approaches to structure-based drug design.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayHumansInsulinLigandsMolecular Dynamics SimulationProtein BindingProtein ConformationProtein MultimerizationReceptor, InsulinSignal TransductionInsulinLigandsReceptor, Insulin

Identifiers

PMID31727777
PMCPMC7039211

What OpenQuestion holds

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LicenceCC BY
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.