Evidence map›Paper›PMID 22753930›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2012

The peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics.

Michael G Mage, Michael A Dolan, Rui Wang, Lisa F Boyd, Maria Jamela Revilleza, Howard Robinson, Kannan Natarajan, Nancy B Myers, Ted H Hansen, David H Margulies

Open access · greenAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

43 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Open MHC Class I Conformers: A Look through the Looking Glass.International journal of molecular sciences · 2021
    Review
  15. Article
  16. Article
  17. Review
  18. Markov state modeling reveals alternative unbinding pathways for peptide-MHC complexes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Review
  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

10 authors at 4 institutions in 1 country.

Michael G MageMolecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. mmage@mail.nih.gov
Michael A Dolan
Rui Wang
Lisa F Boyd
Maria Jamela Revilleza
Howard Robinson
Kannan Natarajan
Nancy B Myers
Ted H Hansen
David H Margulies
National Institute of Allergy and Infectious Diseases · USNational Institutes of Health · USWashington University in St. Louis · USNational Synchrotron Light Source II

Funding

Molecular Genetic Analysis Of Lymphocyte FunctionZIAAI000394 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MARGULIES, DAVID · 2009 to 2025
$11.5M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
MHC-I regulation by herpes virusR01AI019687 · NIAID · WASHINGTON UNIVERSITY · PI FREMONT, DAVED H. · 1985 to 2016
$5.2M
Intramural NIH HHS ZIA AI000394NIAID NIH HHS AI019687NIAID NIH HHS R01 AI019687NIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

MHC class I (MHC-I) proteins of the adaptive immune system require antigenic peptides for maintenance of mature conformation and immune function via specific recognition by MHC-I-restricted CD8(+) T lymphocytes. New MHC-I molecules in the endoplasmic reticulum are held by chaperones in a peptide-receptive (PR) transition state pending release by tightly binding peptides. In this study, we show, by crystallographic, docking, and molecular dynamics methods, dramatic movement of a hinged unit containing a conserved 3(10) helix that flips from an exposed "open" position in the PR transition state to a "closed" position with buried hydrophobic side chains in the peptide-loaded mature molecule. Crystallography of hinged unit residues 46-53 of murine H-2L(d) MHC-I H chain, complexed with mAb 64-3-7, demonstrates solvent exposure of these residues in the PR conformation. Docking and molecular dynamics predict how this segment moves to help form the A and B pockets crucial for the tight peptide binding needed for stability of the mature peptide-loaded conformation, chaperone dissociation, and Ag presentation.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceAnimalsbeta 2-MicroglobulinCrystallography, X-RayH-2 AntigensHistocompatibility Antigen H-2DHumansLigandsMiceMolecular Sequence DataPeptide FragmentsStructure-Activity Relationshipbeta 2-MicroglobulinH-2 AntigensHistocompatibility Antigen H-2DLigandsPeptide Fragments

Identifiers

PMID22753930
PMCPMC3422668
OpenAlexW2147514865

What OpenQuestion holds

Textmetadata
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.