Evidence map›Paper›PMID 11148219›Full record

ArticleThe Journal of experimental medicine2001

The functional binding site for the C-type lectin-like natural killer cell receptor Ly49A spans three domains of its major histocompatibility complex class I ligand.

N Matsumoto, M Mitsuki, K Tajima, W M Yokoyama, K Yamamoto

Abstract read
In one paragraph

Article in The Journal of experimental medicine, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Natural killer cell licensing in mice with inducible expression of MHC class I.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Effects of MHC class I alleles on licensing of Ly49A+ NK cells.Journal of immunology (Baltimore, Md. : 1950) · 2010
    Article
  13. Article
  14. Essential role of the Ly49A stalk region for immunological synapse formation and signaling.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  15. Article
  16. Review
  17. Stable masking by H-2Dd cis ligand limits Ly49A relocalization to the site of NK cell/target cell contact.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Review
  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

5 authors.

N MatsumotoLaboratory of Molecular Medicine, Department of Integrated Biosciences, The University of Tokyo Graduate School of Frontier Sciences, Tokyo 113-0033, Japan. nmatsu@k.u-tokyo.ac.jp
M Mitsuki
K Tajima
W M Yokoyama
K Yamamoto

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural killer (NK) cells express receptors that recognize major histocompatibility complex (MHC) class I molecules and regulate cytotoxicity of target cells. In this study, we demonstrate that Ly49A, a prototypical C-type lectin-like receptor expressed on mouse NK cells, requires species-specific determinants on beta2-microglobulin (beta2m) to recognize its mouse MHC class I ligand, H-2D(d). The involvement of beta2m in the interaction between Ly49A and H-2D(d) is also demonstrated by the functional effects of a beta2m-specific antibody. We also define three residues in alpha1/alpha2 and alpha3 domains of H-2D(d) that are critical for the recognition of H-2D(d) on target cells by Ly49A. In the crystal structure of the Ly49A/H-2D(d) complex, these residues are involved in hydrogen bonding to Ly49A in one of the two potential Ly49A binding sites on H-2D(d). These data unambiguously indicate that the functional effect of Ly49A as an MHC class I-specific NK cell receptor is mediated by binding to a concave region formed by three structural domains of H-2D(d), which partially overlaps the CD8 binding site.

Indexed as

Antigens, LyAnimalsBase Sequencebeta 2-MicroglobulinBinding SitesCarrier ProteinsCD8 AntigensCell LineDNA PrimersH-2 AntigensHistocompatibility Antigen H-2DHumansIn Vitro TechniquesKiller Cells, NaturalLectinsLectins, C-TypeAntigens, Lybeta 2-MicroglobulinCarrier ProteinsCD8 AntigensDNA PrimersH-2 AntigensHistocompatibility Antigen H-2DKlra1 protein, mouseLectinsLectins, C-TypeLigandsMacromolecular SubstancesMembrane ProteinsNK Cell Lectin-Like Receptor Subfamily AReceptors, ImmunologicReceptors, NK Cell Lectin-Like

Identifiers

PMID11148219
PMCPMC2193338

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Registered trials

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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.