ReviewThe Biochemical journal2008
Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes.
Review in The Biochemical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
What it found
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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.
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.
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Who cites it
74 citing papers in PubMed, 117 citations in OpenAlex.
- Dynamic Allostery in T Cell Receptor Specificity: A Role for Peptides and MHC Polymorphisms in Allosterically Tuning Immune Recognition.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Dynamical network analysis reveals long-range residue couplings at the pMHC interface underlying enhanced immunogenicity.NPJ systems biology and applications · 2026Article
- Deep Mutational Scanning in Immunology: Techniques and Applications.Pathogens (Basel, Switzerland) · 2025Review
- AI-driven epitope prediction: a system review, comparative analysis, and practical guide for vaccine development.NPJ vaccines · 2025Review
- TCR repertoire of human cytotoxic CD4 T cells responding to betaherpesviruses HHV-6B and HCMV.Frontiers in immunology · 2025Article
- Quantifying conformational changes in the TCR:pMHC-I binding interface.Frontiers in immunology · 2024Article
- Enhanced T cell receptor specificity through framework engineering.Frontiers in immunology · 2024Article
- Conformational flexibility of a free and TCR-bound pMHC-I protein investigated by long-term molecular dynamics simulations.BMC immunology · 2022Article
- Challenges in describing the conformation and dynamics of proteins with ambiguous behavior.Frontiers in molecular biosciences · 2022Article
- Structural plasticity in I-AFrontiers in immunology · 2022Article
- Immunological Mechanisms of Metal Allergies and the Nickel-Specific TCR-pMHC Interface.International journal of environmental research and public health · 2021Review
- Structure of Blood Coagulation Factor VIII in Complex With an Anti-C2 Domain Non-Classical, Pathogenic Antibody Inhibitor.Frontiers in immunology · 2021Article
- Peptide cargo tunes a network of correlated motions in human leucocyte antigens.The FEBS journal · 2020Article
- T cell receptor interactions with human leukocyte antigen govern indirect peptide selectivity for the cancer testis antigen MAGE-A4.The Journal of biological chemistry · 2020Article
- Conformational Plasticity of HLA-B27 Molecules Correlates Inversely With Efficiency of Negative T Cell Selection.Frontiers in immunology · 2020Article
- Article
- TCR-induced alteration of primary MHC peptide anchor residue.European journal of immunology · 2019Article
- Immune aging in diabetes and its implications in wound healing.Clinical immunology (Orlando, Fla.) · 2019Review
- Peripheral T cell receptor beta immune repertoire is promptly reconstituted after acute myocardial infarction.Journal of translational medicine · 2019Article
- Dual HLA B*42 and B*81-reactive T cell receptors recognize more diverse HIV-1 Gag escape variants.Nature communications · 2018Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A necessary feature of the immune system, TCR (T-cell receptor) cross-reactivity has been implicated in numerous autoimmune pathologies and is an underlying cause of transplant rejection. Early studies of the interactions of alphabeta TCRs (T-cell receptors) with their peptide-MHC ligands suggested that conformational plasticity in the TCR CDR (complementarity determining region) loops is a dominant contributor to T-cell cross-reactivity. Since these initial studies, the database of TCRs whose structures have been solved both bound and free is now large enough to permit general conclusions to be drawn about the extent of TCR plasticity and the types and locations of motion that occur. In the present paper, we review the conformational differences between free and bound TCRs, quantifying the structural changes that occur and discussing their possible roles in specificity and cross-reactivity. We show that, rather than undergoing major structural alterations or 'folding' upon binding, the majority of TCR CDR loops shift by relatively small amounts. The structural changes that do occur are dominated by hinge-bending motions, with loop remodelling usually occurring near loop apexes. As predicted from previous studies, the largest changes are in the hypervariable CDR3alpha and CDR3beta loops, although in some cases the germline-encoded CDR1alpha and CDR2alpha loops shift in magnitudes that approximate those of the CDR3 loops. Intriguingly, the smallest shifts are in the germline-encoded loops of the beta-chain, consistent with recent suggestions that the TCR beta domain may drive ligand recognition.
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Registered trials
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.