Evidence map›Paper›PMID 27791034›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

A conserved αβ transmembrane interface forms the core of a compact T-cell receptor-CD3 structure within the membrane.

Logesvaran Krshnan, Soohyung Park, Wonpil Im, Melissa J Call, Matthew E Call

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. 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
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Focusing on CD8Journal of experimental & clinical cancer research : CR · 2024
    Review
  7. Article
  8. Article
  9. What's the Catch? The Significance of Catch Bonds in T Cell Activation.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  10. Article
  11. Article
  12. Review
  13. T cell and B cell antigen receptors share a conserved core transmembrane structure.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Structural understanding of T cell receptor triggering.Cellular & molecular immunology · 2020
    Review
  19. Article
  20. T Cell Reprogramming Against Cancer.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
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 at 3 institutions in 2 countries.

Logesvaran KrshnanStructural Biology Division, Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3052, Australia.
Soohyung ParkDepartment of Biological Sciences and Bioengineering Program, Lehigh University, Bethlehem, PA 18015.
Wonpil ImDepartment of Biological Sciences and Bioengineering Program, Lehigh University, Bethlehem, PA 18015.
Melissa J CallStructural Biology Division, Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3052, Australia; call@wehi.edu.au.
Matthew E CallStructural Biology Division, Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3052, Australia; call@wehi.edu.au.
Lehigh University · USUniversity of Melbourne · AUWalter and Eliza Hall Institute of Medical Research · AU

Funding

Mechanisms & Energetics of Transmembrane-induced Signaling of Cytokine ReceptorsR01GM092950 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI IM, WONPIL · 2010 to 2014
$1.4M
Medical Research CouncilNIGMS NIH HHS R01 GM092950
6 · The paper itself

Abstract

The T-cell antigen receptor (TCR) is an assembly of eight type I single-pass membrane proteins that occupies a central position in adaptive immunity. Many TCR-triggering models invoke an alteration in receptor complex structure as the initiating event, but both the precise subunit organization and the pathway by which ligand-induced alterations are transferred to the cytoplasmic signaling domains are unknown. Here, we show that the receptor complex transmembrane (TM) domains form an intimately associated eight-helix bundle organized by a specific interhelical TCR TM interface. The salient features of this core structure are absolutely conserved between αβ and γδ TCR sequences and throughout vertebrate evolution, and mutations at key interface residues caused defects in the formation of stable TCRαβ:CD3δε:CD3γε:ζζ complexes. These findings demonstrate that the eight TCR-CD3 subunits form a compact and precisely organized structure within the membrane and provide a structural basis for further investigation of conformationally regulated models of transbilayer TCR signaling.

Indexed as

Amino Acid SequenceBinding SitesCD3 ComplexCell MembraneCrystallography, X-RayEscherichia coliGene ExpressionHumansMolecular Dynamics SimulationProtein BindingProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsProtein SubunitsReceptor-CD3 Complex, Antigen, T-CellReceptors, Antigen, T-Cell, alpha-betaReceptors, Antigen, T-Cell, gamma-deltaCD3 ComplexProtein SubunitsReceptor-CD3 Complex, Antigen, T-CellReceptors, Antigen, T-Cell, alpha-betaReceptors, Antigen, T-Cell, gamma-deltaRecombinant Proteinscysteine cross-linkingMD simulationNMRT-cell receptortransmembrane structure

Identifiers

PMID27791034
PMCPMC5086997
OpenAlexW2530702450

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.