Evidence map›Paper›PMID 8692965›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Direct binding of a soluble natural killer cell inhibitory receptor to a soluble human leukocyte antigen-Cw4 class I major histocompatibility complex molecule.

Q R Fan, D N Garboczi, C C Winter, N Wagtmann, E O Long, D C Wiley

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
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  3. Current strategies for protein production and purification enabling membrane protein structural biology.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
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  17. The role of zinc in the binding of killer cell Ig-like receptors to class I MHC proteins.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  18. Article
  19. Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  20. Differential binding to HLA-C of p50-activating and p58-inhibitory natural killer cell receptors.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

6 authors at 1 institution in 1 country.

Q R FanDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
D N Garboczi
C C Winter
N Wagtmann
E O Long
D C Wiley
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural killer (NK) cells expressing specific p58 NK receptors are inhibited from lysing target cells that express human leukocyte antigen (HLA)-C class I major histocompatibility complex molecules. To investigate the interaction between p58 NK receptors and HLA-Cw4, the extracellular domain of the p58 NK receptor specific for HLA-Cw4 was overexpressed in Escherichia coli and refolded from purified inclusion bodies. The refolded NK receptor is a monomer in solution. It interacts specifically with HLA-Cw4, blocking the binding of a p58-Ig fusion protein to HLA-Cw4-expressing cells, but does not block the binding of a p58-Ig fusion protein specific for HLA-Cw3 to HLA-Cw3-expressing cells. The bacterially expressed extracellular domain of HLA-Cw4 heavy chain and beta2-microglobulin were refolded in the presence of a HLA-Cw4-specific peptide. Direct binding between the soluble p58 NK receptor and the soluble HLA-Cw4-peptide complex was observed by native gel electrophoresis. Titration binding assays show that soluble monomeric receptor forms a 1:1 complex with HLA-Cw4, independent of the presence of Zn2+. The formation of complexes between soluble, recombinant molecules indicates that HLA-Cw4 is sufficient for specific ligation by the NK receptor and that neither glycoprotein requires carbohydrate for the interaction.

Indexed as

Amino Acid SequenceBase Sequencebeta 2-MicroglobulinChromatography, GelDNA PrimersHLA-C AntigensHumansInclusion BodiesKiller Cells, NaturalMacromolecular SubstancesMolecular Sequence DataPolymerase Chain ReactionProtein BindingProtein Sorting SignalsReceptors, ImmunologicReceptors, KIRbeta 2-MicroglobulinDNA PrimersHLA-C*04 antigenHLA-C AntigensKIR2DL3 protein, humanMacromolecular SubstancesProtein Sorting SignalsReceptors, ImmunologicReceptors, KIRReceptors, KIR2DL3Recombinant Fusion Proteins

Identifiers

PMID8692965
PMCPMC38956
OpenAlexW1972777763

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.