Evidence map›Paper›PMID 21422170›Full record

ArticleThe Journal of experimental medicine2011

Structure of the human activating natural cytotoxicity receptor NKp30 bound to its tumor cell ligand B7-H6.

Yili Li, Qian Wang, Roy A Mariuzza

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

68 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. NKp30: A Key Membrane Molecule in the Fight Against Cancer and Infection.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  7. Article
  8. Article
  9. Enhancing NK cell-mediated tumor killing of B7-H6Molecular therapy. Oncology · 2025
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. A Novel B7-H6-Targeted IgG-Like T Cell-Engaging Antibody for the Treatment of Gastrointestinal Tumors.Clinical cancer research : an official journal of the American Association for Cancer Research · 2022
    Article
  18. Article
  19. Frontiers in medicine · 2022
    Article
  20. Review

8 more citing papers are in PubMed but not listed here.

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.

Yili LiWM Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA.
Qian Wang
Roy A Mariuzza
University of Maryland, College Park · USInstitute for Bioscience and Biotechnology Research

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
STRUCTURE AND FUNCTION OF NATURAL KILLER CELL RECEPTORSR01AI047990 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI MARIUZZA, ROY A · 2000 to 2014
$4.1M
NIAID NIH HHS AI047990NIAID NIH HHS R01 AI047990NIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

Natural killer (NK) cells are lymphocytes of the innate immune system that participate in the elimination of tumor cells. In humans, the activating natural cytotoxicity receptors (NCRs) NKp30, NKp44, and NKp46 play a major role in NK cell-mediated tumor cell lysis. NKp30 recognizes B7-H6, a member of the B7 family which is expressed on tumor, but not healthy, cells. To understand the basis for tumor surveillance by NCRs, we determined the structure of NKp30, a member of the CD28 family which includes CTLA-4 and PD-1, in complex with B7-H6. The overall organization of the NKp30-B7-H6-activating complex differs considerably from those of the CTLA-4-B7 and PD-1-PD-L T cell inhibitory complexes. Whereas CTLA-4 and PD-1 use only the front β-sheet of their Ig-like domain to bind ligands, NKp30 uses both front and back β-sheets, resulting in engagement of B7-H6 via the side, as well as face, of the β-sandwich. Moreover, B7-H6 contacts NKp30 through the complementarity-determining region (CDR)-like loops of its V-like domain in an antibody-like interaction that is not observed for B7 or PD-L. This first structure of an NCR bound to ligand provides a template for designing molecules to stimulate NKp30-mediated cytolytic activity for tumor immunotherapy.

Indexed as

Amino Acid SequenceAntigens, CDApoptosis Regulatory ProteinsB7-1 AntigenB7 AntigensCTLA-4 AntigenHumansModels, MolecularMolecular Sequence DataNatural Cytotoxicity Triggering Receptor 3Programmed Cell Death 1 ReceptorProtein BindingProtein Structure, QuaternaryProtein Structure, SecondarySequence AlignmentSurface Plasmon ResonanceAntigens, CDApoptosis Regulatory ProteinsB7-1 AntigenB7 AntigensCTLA-4 AntigenCTLA4 protein, humanNatural Cytotoxicity Triggering Receptor 3NCR3LG1 protein, humanNCR3 protein, humanPDCD1 protein, humanProgrammed Cell Death 1 Receptor

Identifiers

PMID21422170
PMCPMC3135353
OpenAlexW2038016611

What OpenQuestion holds

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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.