Evidence map›Paper›PMID 32788370›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Atomistic structure and dynamics of the human MHC-I peptide-loading complex.

Olivier Fisette, Gunnar F Schröder, Lars V Schäfer

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 53 citations in OpenAlex.

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  9. Article
  10. Review
  11. Crystal structure ofFrontiers in immunology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Effects of calreticulin mutations on cell transformation and immunity.Journal of cellular and molecular medicine · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. A guide to antigen processing and presentation.Nature reviews. Immunology · 2022
    Review
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

3 authors at 2 institutions in 1 country.

Olivier FisetteTheoretical Chemistry, Ruhr University Bochum, D-44780 Bochum, Germany.ORCID 0000-0002-8043-4655
Gunnar F SchröderInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, D-52425 Jülich, Germany.
Lars V SchäferTheoretical Chemistry, Ruhr University Bochum, D-44780 Bochum, Germany; Lars.Schaefer@ruhr-uni-bochum.de.ORCID 0000-0002-8498-3061
Ruhr University Bochum · DEForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major histocompatibility complex class-I (MHC-I) peptide-loading complex (PLC) is a cornerstone of the human adaptive immune system, being responsible for processing antigens that allow killer T cells to distinguish between healthy and compromised cells. Based on a recent low-resolution cryo-electron microscopy (cryo-EM) structure of this large membrane-bound protein complex, we report an atomistic model of the PLC and study its conformational dynamics on the multimicrosecond time scale using all-atom molecular dynamics (MD) simulations in an explicit lipid bilayer and water environment (1.6 million atoms in total). The PLC has a layered structure, with two editing modules forming a flexible protein belt surrounding a stable, catalytically active core. Tapasin plays a central role in the PLC, stabilizing the MHC-I binding groove in a conformation reminiscent of antigen-loaded MHC-I. The MHC-I-linked glycan steers a tapasin loop involved in peptide editing toward the binding groove. Tapasin conformational dynamics are also affected by calreticulin through a conformational selection mechanism that facilitates MHC-I recruitment into the complex.

Indexed as

CalreticulinCryoelectron MicroscopyHistocompatibility Antigens Class IHumansMembrane Transport ProteinsMolecular Dynamics SimulationPolysaccharidesProtein Disulfide-IsomerasesCalreticulinHistocompatibility Antigens Class IMembrane Transport ProteinsPDIA3 protein, humanPolysaccharidesProtein Disulfide-IsomerasestapasinimmunityMHC-Imolecular dynamics simulationspeptide-loading complexprotein dynamics

Identifiers

PMID32788370
PMCPMC7456110
OpenAlexW3048920300

What OpenQuestion holds

Textmetadata
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.