Evidence map›Paper›PMID 22101157›Full record

ArticleImmunity2011

T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex.

Jarrett J Adams, Samanthi Narayanan, Baoyu Liu, Michael E Birnbaum, Andrew C Kruse, Natalie A Bowerman, Wei Chen, Aron M Levin, Janet M Connolly, Cheng Zhu and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 176 papers.

0numbers the graph read from it
0cells of the map it votes in
176citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

176 citing papers in PubMed, 261 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. High-throughput screening for class I peptide MHC binding via yeast surface display.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Strengths and limitations of web servers for the modeling of TCRpMHC complexes.Computational and structural biotechnology journal · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Molecular basis for antibody recognition of multiple drug-peptide/MHC complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

116 more citing papers are in PubMed but not listed here.

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

12 authors at 4 institutions in 1 country.

Jarrett J AdamsHoward Hughes Medical Institute, and Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Samanthi Narayanan
Baoyu Liu
Michael E Birnbaum
Andrew C Kruse
Natalie A Bowerman
Wei Chen
Aron M Levin
Janet M Connolly
Cheng Zhu
David M Kranz
K Christopher Garcia
Howard Hughes Medical Institute · USGeorgia Institute of Technology · USUniversity of Illinois Urbana-Champaign · USWashington University in St. Louis · US

Funding

Molecular Principles of TCR Recognition and Activation by peptide-MHCR01AI048540 · NIAID · STANFORD UNIVERSITY · PI GARCIA, KENAN CHRISTOPHER · 2001 to 2010
$2.9M
Structure, Function &Engineering of Tau Cell ReceptorsR01GM055767 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KRANZ, DAVID M. · 1997 to 2009
$2.4M
Molecular Principles of TCR Recognition and Activation by Peptide MHCR56AI048540 · NIAID · STANFORD UNIVERSITY · PI GARCIA, KENAN CHRISTOPHER · 2011 to 2011
$395k
CIHRHoward Hughes Medical InstituteNIAID NIH HHS AI48540NIAID NIH HHS R01 AI048540NIAID NIH HHS R56 AI048540NIGMS NIH HHS GM55767NIGMS NIH HHS R01 GM055767
6 · The paper itself

Abstract

T cell receptor (TCR) engagement of peptide-major histocompatibility complex (pMHC) is essential to adaptive immunity, but it is unknown whether TCR signaling responses are influenced by the binding topology of the TCR-peptide-MHC complex. We developed yeast-displayed pMHC libraries that enabled us to identify new peptide sequences reactive with a single TCR. Structural analysis showed that four peptides bound to the TCR with distinct 3D and 2D affinities using entirely different binding chemistries. Three of the peptides that shared a common docking mode, where key TCR-MHC germline interactions are preserved, induced TCR signaling. The fourth peptide failed to induce signaling and was recognized in a substantially different TCR-MHC binding mode that apparently exceeded geometric tolerances compatible with signaling. We suggest that the stereotypical TCR-MHC docking paradigm evolved from productive signaling geometries and that TCR signaling can be modulated by peptides that are recognized in alternative TCR-pMHC binding orientations.

Indexed as

Signal TransductionAmino Acid MotifsAmino Acid SequenceAnimalsEpitopes, T-LymphocyteHistocompatibility Antigens Class IHumansLymphocyte ActivationMiceModels, MolecularPeptide LibraryPeptidesProtein BindingProtein ConformationReceptors, Antigen, T-CellReproducibility of ResultsEpitopes, T-LymphocyteHistocompatibility Antigens Class IPeptide LibraryPeptidesReceptors, Antigen, T-Cell

Identifiers

PMID22101157
PMCPMC3253265
OpenAlexW2038509173

What OpenQuestion holds

Textmetadata
LicenceTDM
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.