ArticleJournal of immunology (Baltimore, Md. : 1950)2014
TCR scanning of peptide/MHC through complementary matching of receptor and ligand molecular flexibility.
Article in Journal of immunology (Baltimore, Md. : 1950), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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
44 citing papers in PubMed, 60 citations in OpenAlex.
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Nature communications · 2025Article
- The Evolving T Cell Receptor Recognition Code: The Rules Are More Like Guidelines.Immunological reviews · 2025Review
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Research square · 2024Article
- 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
- The Energetic Landscape of Catch Bonds in TCR Interfaces.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- Identification of HLA-E BindingJournal of immunology (Baltimore, Md. : 1950) · 2022Article
- Article
- Unconventional modes of peptide-HLA-I presentation change the rules of TCR engagement.Discovery immunology · 2022Review
- TCR mimic compounds for pHLA targeting with high potency modalities in oncology.Frontiers in oncology · 2022Review
- Identification and validation of viral antigens sharing sequence and structural homology with tumor-associated antigens (TAAs).Journal for immunotherapy of cancer · 2021Article
- Identification and characterization of heteroclitic peptides in TCR-binding positions with improved HLA-binding efficacy.Journal of translational medicine · 2021Article
- MHC-Optimized Peptide Scaffold for Improved Antigen Presentation and Anti-Tumor Response.Frontiers in immunology · 2021Article
- Selecting Target Antigens for Cancer Vaccine Development.Vaccines · 2020Review
- 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
- TCRs with Distinct Specificity Profiles Use Different Binding Modes to Engage an Identical Peptide-HLA Complex.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Structural understanding of T cell receptor triggering.Cellular & molecular immunology · 2020Review
- Article
- The Role of Conformational Dynamics in Abacavir-Induced Hypersensitivity Syndrome.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
Although conformational changes in TCRs and peptide Ags presented by MHC protein (pMHC) molecules often occur upon binding, their relationship to intrinsic flexibility and role in ligand selectivity are poorly understood. In this study, we used nuclear magnetic resonance to study TCR-pMHC binding, examining recognition of the QL9/H-2L(d) complex by the 2C TCR. Although the majority of the CDR loops of the 2C TCR rigidify upon binding, the CDR3β loop remains mobile within the TCR-pMHC interface. Remarkably, the region of the QL9 peptide that interfaces with CDR3β is also mobile in the free pMHC and in the TCR-pMHC complex. Determination of conformational exchange kinetics revealed that the motions of CDR3β and QL9 are closely matched. The matching of conformational exchange in the free proteins and its persistence in the complex enhances the thermodynamic and kinetic stability of the TCR-pMHC complex and provides a mechanism for facile binding. We thus propose that matching of structural fluctuations is a component of how TCRs scan among potential ligands for those that can bind with sufficient stability to enable T cell signaling.
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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.