Evidence map›Paper›PMID 10200255›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution.

S Ikemizu, L M Sparks, P A van der Merwe, K Harlos, D I Stuart, E Y Jones, S J Davis

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. CD58 Immunobiology at a Glance.Frontiers in immunology · 2021
    Review
  7. Article
  8. CD2 Immunobiology.Frontiers in immunology · 2020
    Review
  9. Article
  10. Linking 3D and 2D binding kinetics of membrane proteins by multiscale simulations.Protein science : a publication of the Protein Society · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Perspective on computational simulations of glycosaminoglycans.Wiley interdisciplinary reviews. Computational molecular science
    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

7 authors at 2 institutions in 1 country.

S IkemizuLaboratory of Molecular Biophysics, the Rex Richards Building, South Parks Road, Oxford, OX1 3QU, United Kingdom.
L M Sparks
P A van der Merwe
K Harlos
D I Stuart
E Y Jones
S J Davis
John Radcliffe Hospital · GBMedical Research Council · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The binding of the cell surface molecule CD58 (formerly lymphocyte function-associated antigen 3) to its ligand, CD2, significantly increases the sensitivity of antigen recognition by T cells. This was the first heterophilic cell adhesion interaction to be discovered and is now an important paradigm for analyzing the structural basis of cell-cell recognition. The crystal structure of a CD2-binding chimeric form of CD58, solved to 1.8-A resolution, reveals that the ligand binding domain of CD58 has the expected Ig superfamily V-set topology and shares several of the hitherto unique structural features of CD2, consistent with previous speculation that the genes encoding these molecules arose via duplication of a common precursor. Nevertheless, evidence for considerable divergence of CD2 and CD58 is also implicit in the structures. Mutations that disrupt CD2 binding map to the highly acidic surface of the AGFCC'C" beta-sheet of CD58, which, unexpectedly, lacks marked shape complementarity to the equivalent, rather more basic CD58-binding face of human CD2. The specificity of the very weak interactions of proteins mediating cell-cell recognition may often derive largely from electrostatic complementarity, with shape matching at the protein-protein interface being less exact than for interactions that combine specificity with high affinity, such as those involving antibodies.

Indexed as

Amino Acid SequenceAnimalsAntigen-Antibody ComplexAntigens, CDBinding SitesCD2 AntigensCD58 AntigensCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataProtein Structure, SecondaryRatsSequence AlignmentSequence Homology, Amino AcidAntigen-Antibody ComplexAntigens, CDCD2 AntigensCD58 Antigens

Identifiers

PMID10200255
PMCPMC16325
OpenAlexW2049090751

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.