Evidence map›Paper›PMID 21788486›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Crystal structure of human CD1e reveals a groove suited for lipid-exchange processes.

Luis F Garcia-Alles, Gaelle Giacometti, Cees Versluis, Laurent Maveyraud, Diane de Paepe, Julie Guiard, Samuel Tranier, Martine Gilleron, Jacques Prandi, Daniel Hanau and 6 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Detergents alter the stability and lipid binding properties of the CD1d immunoreceptor.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Trafficking ofFrontiers in immunology · 2020
    Review
  11. Review
  12. Review
  13. Molecular recognition of microbial lipid-based antigens by T cells.Cellular and molecular life sciences : CMLS · 2018
    Review
  14. Article
  15. CD1: A Singed Cat of the Three Antigen Presentation Systems.Archivum immunologiae et therapiae experimentalis · 2017
    Review
  16. Review
  17. Review
  18. Review
  19. Cholesteryl esters stabilize human CD1c conformations for recognition by self-reactive T cells.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. 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

16 authors at 7 institutions in 4 countries.

Luis F Garcia-AllesCentre National de la Recherche Scientifique, Institut de Pharmacologie et de Biologie Structurale, Toulouse F-31077, France.
Gaelle Giacometti
Cees Versluis
Laurent Maveyraud
Diane de Paepe
Julie Guiard
Samuel Tranier
Martine Gilleron
Jacques Prandi
Daniel Hanau
Albert J R Heck
Lucia Mori
Gennaro De Libero
Germain Puzo
Lionel Mourey
Henri de la Salle
Université Fédérale de Toulouse Midi-Pyrénées · FRÉtablissement Français du Sang · FRInstitut de Pharmacologie et de Biologie Structurale · FRUtrecht University · NLSingapore Immunology Network · SGUniversité Toulouse III - Paul Sabatier · FRUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CD1e is the only human CD1 protein existing in soluble form in the late endosomes of dendritic cells, where it facilitates the processing of glycolipid antigens that are ultimately recognized by CD1b-restricted T cells. The precise function of CD1e remains undefined, thus impeding efforts to predict the participation of this protein in the presentation of other antigens. To gain insight into its function, we determined the crystal structure of recombinant CD1e expressed in human cells at 2.90-Å resolution. The structure revealed a groove less intricate than in other CD1 proteins, with a significantly wider portal characterized by a 2 Å-larger spacing between the α1 and α2 helices. No electron density corresponding to endogenous ligands was detected within the groove, despite the presence of ligands unequivocally established by native mass spectrometry in recombinant CD1e. Our structural data indicate that the water-exposed CD1e groove could ensure the establishment of loose contacts with lipids. In agreement with this possibility, lipid association and dissociation processes were found to be considerably faster with CD1e than with CD1b. Moreover, CD1e was found to mediate in vitro the transfer of lipids to CD1b and the displacement of lipids from stable CD1b-antigen complexes. Altogether, these data support that CD1e could have evolved to mediate lipid-exchange/editing processes with CD1b and point to a pathway whereby the repertoire of lipid antigens presented by human dendritic cells might be expanded.

Indexed as

Lipid MetabolismAcylationAntigens, CD1Crystallography, X-RayHumansLigandsLipidsModels, MolecularProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryAntigens, CD1CD1b antigenCD1e antigenLigandsLipids

Identifiers

PMID21788486
PMCPMC3156185
OpenAlexW2106636892

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.