Evidence map›Paper›PMID 17023417›Full record

ArticleThe Journal of biological chemistry2006

A membrane-proximal tetracysteine motif contributes to assembly of CD3deltaepsilon and CD3gammaepsilon dimers with the T cell receptor.

Chenqi Xu, Matthew E Call, Kai W Wucherpfennig

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Structural understanding of T cell receptor triggering.Cellular & molecular immunology · 2020
    Review
  6. Article
  7. Article
  8. Ionic CD3-Lck interaction regulates the initiation of T-cell receptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Article
  11. A conserved αβ transmembrane interface forms the core of a compact T-cell receptor-CD3 structure within the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Molecular architecture of the αβ T cell receptor-CD3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

3 authors.

Chenqi XuDepartment of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Matthew E Call
Kai W Wucherpfennig

Funding

Structural Determinants of TCR Assembly and SignalingR01AI054520 · NIAID · DANA-FARBER CANCER INSTITUTE · PI WUCHERPFENNIG, KAI W · 2003 to 2013
$4.0M
NIAID NIH HHS R01 AI054520
6 · The paper itself

Abstract

Assembly of the T cell receptor (TCR) with its dimeric signaling modules, CD3deltaepsilon, CD3gammaepsilon, and zetazeta, is organized by transmembrane (TM) interactions. Each of the three assembly steps requires formation of a three-helix interface involving one particular basic TCR TM residue and two acidic TM residues of the respective signaling dimer. The extracellular domains of CD3deltaepsilon and CD3gammaepsilon contribute to assembly, but TCR interaction sites on CD3 dimers have not been defined. The structures of the extracellular domains of CD3deltaepsilon and CD3gammaepsilon demonstrated parallel beta-strands ending at the first cysteine in the CXXCXEXXX motif present in the stalk segment of each CD3 chain. Mutation of the membrane-proximal cysteines impaired assembly of either CD3 dimer with TCR, and little complex was isolated when all four membrane-proximal cysteines were mutated to alanine. These mutations had, however, no discernable effect on CD3deltaepsilon or CD3gammaepsilon dimerization. CD3deltaepsilon assembled with a TCRalpha mutant that lacked both immunoglobulin domains, but shortening of the TCRalpha connecting peptide reduced assembly, consistent with membrane-proximal TCRalpha-CD3deltaepsilon interactions. Chelation of divalent cations did not affect assembly, indicating that coordination of a cation by the tetracysteine motif was not required. The membrane-proximal cysteines were within close proximity but only formed covalent CD3 dimers when one cysteine was mutated. The four cysteines may thus form two intrachain disulfide bonds integral to the secondary structure of CD3 stalk regions. The three-chain interaction theme first established for the TM domains thus extends into the membrane-proximal domains of TCRalpha-CD3deltaepsilon and TCRbeta-CD3gammaepsilon.

Indexed as

Amino Acid MotifsAmino Acid SequenceCD3 ComplexDimerizationHumansMolecular Sequence DataProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Antigen, T-CellSequence Homology, Amino AcidTetracyclineCD3 antigen, gamma chainCD3 antigen, zeta chainCD3 ComplexCD3delta antigenCD3E protein, humanReceptors, Antigen, T-CellTetracycline

Identifiers

PMID17023417
PMCPMC4515964

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.