Evidence map›Paper›PMID 14734527›Full record

ArticleThe Journal of experimental medicine2004

Dual, HLA-B27 subtype-dependent conformation of a self-peptide.

Martin Hülsmeyer, Maria Teresa Fiorillo, Francesca Bettosini, Rosa Sorrentino, Wolfram Saenger, Andreas Ziegler, Barbara Uchanska-Ziegler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
5.7field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 143 citations in OpenAlex.

  1. Guideline
  2. Review
  3. Article
  4. Spondyloarthritides: Theories and beyond.Frontiers in pediatrics · 2022
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. How an alloreactive T-cell receptor achieves peptide and MHC specificity.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Editorial: HLA-B27: The Story Continues to Unfold.Arthritis & rheumatology (Hoboken, N.J.) · 2016
    Article
  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

7 authors at 3 institutions in 2 countries.

Martin HülsmeyerInstitut für Kristallographie, Freie Universität Berlin, 14195 Berlin, Germany.
Maria Teresa Fiorillo
Francesca Bettosini
Rosa Sorrentino
Wolfram Saenger
Andreas Ziegler
Barbara Uchanska-Ziegler
Sapienza University of Rome · ITCharité - Universitätsmedizin Berlin · DEFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The products of the human leukocyte antigen subtypes HLA-B*2705 and HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide binding groove but are differentially associated with the autoimmune disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T cell repertoires as exemplified by distinct T cell responses against the self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705 molecules. In one binding mode, peptide pArg5 forms a salt bridge to Asp116, connected with drastically different interactions between peptide and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent differences in pVIPR binding link the emergence of dissimilar T cell repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried Asp116/His116 polymorphism and provide novel insights into peptide presentation by major histocompatibility antigens.

Indexed as

Amino Acid SequenceBinding SitesCell LineHLA-B27 AntigenHLA-B AntigensHumansModels, MolecularProtein BindingProtein ConformationSpondylitis, AnkylosingStatic ElectricityT-Lymphocytes, CytotoxicHLA-B*27:05 antigenHLA-B*27:09 antigenHLA-B27 AntigenHLA-B Antigens

Identifiers

PMID14734527
PMCPMC2211767
OpenAlexW2106319835

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.