Evidence map›Paper›PMID 17563375›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Structure of CD84 provides insight into SLAM family function.

Qingrong Yan, Vladimir N Malashkevich, Alexander Fedorov, Elena Fedorov, Erhu Cao, Jeffrey W Lary, James L Cole, Stanley G Nathenson, Steven C Almo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.0field-weighted citation impact, top 14% 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, 76 citations in OpenAlex.

  1. Article
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  5. Review
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  7. Article
  8. SLAM Family Receptors in B Cell Chronic Lymphoproliferative Disorders.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. SLAMF9 regulates pDC homeostasis and function in health and disease.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Review
  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

9 authors at 3 institutions in 2 countries.

Qingrong YanDepartment of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Vladimir N Malashkevich
Alexander Fedorov
Elena Fedorov
Erhu Cao
Jeffrey W Lary
James L Cole
Stanley G Nathenson
Steven C Almo
University of Connecticut · USAlbert Einstein College of Medicine · USBipar · FR

Funding

Molecular and Structural Basis for T Cell CostimulationR01AI007289 · NIAID · YESHIVA UNIVERSITY · PI NATHENSON, STANLEY G · 1985 to 2012
$7.7M
Molecular and Structural Basis for T Cell CostimulationR56AI007289 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI NATHENSON, STANLEY G · 2007 to 2007
$553k
BIOCHEMICAL STUDIES ON HISTOCOMPATIBILITY ANTIGENSR37AI007289 · NIAID · YESHIVA UNIVERSITY · PI NATHENSON, STANLEY G · 1987 to 1996
–
NIAID NIH HHS AI07289NIAID NIH HHS R01 AI007289NIAID NIH HHS R56 AI007289
6 · The paper itself

Abstract

The signaling lymphocyte activation molecule (SLAM) family includes homophilic and heterophilic receptors that modulate both adaptive and innate immune responses. These receptors share a common ectodomain organization: a membrane-proximal immunoglobulin constant domain and a membrane-distal immunoglobulin variable domain that is responsible for ligand recognition. CD84 is a homophilic family member that enhances IFN-gamma secretion in activated T cells. Our solution studies revealed that CD84 strongly self-associates with a K(d) in the submicromolar range. These data, in combination with previous reports, demonstrate that the SLAM family homophilic affinities span at least three orders of magnitude and suggest that differences in the affinities may contribute to the distinct signaling behavior exhibited by the individual family members. The 2.0 A crystal structure of the human CD84 immunoglobulin variable domain revealed an orthogonal homophilic dimer with high similarity to the recently reported homophilic dimer of the SLAM family member NTB-A. Structural and chemical differences in the homophilic interfaces provide a mechanism to prevent the formation of undesired heterodimers among the SLAM family homophilic receptors. These structural data also suggest that, like NTB-A, all SLAM family homophilic dimers adopt a highly kinked organization spanning an end-to-end distance of approximately 140 A. This common molecular dimension provides an opportunity for all two-domain SLAM family receptors to colocalize within the immunological synapse and bridge the T cell and antigen-presenting cell.

Indexed as

Amino Acid SequenceAntigens, CDConserved SequenceCrystallography, X-RayDimerizationHumansKineticsModels, ChemicalModels, MolecularMolecular Sequence DataPoint MutationProtein Structure, TertiaryReceptors, Cell SurfaceSequence Homology, Amino AcidSignaling Lymphocytic Activation Molecule FamilySignaling Lymphocytic Activation Molecule Family Member 1Antigens, CDCD84 protein, humanReceptors, Cell SurfaceSignaling Lymphocytic Activation Molecule FamilySignaling Lymphocytic Activation Molecule Family Member 1SLAMF6 protein, human

Identifiers

PMID17563375
PMCPMC1965556
OpenAlexW1972200894

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.