ReviewJournal of molecular recognition : JMR
Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities.
Review in Journal of molecular recognition : JMR. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 68 citations in OpenAlex.
- Mechanotransduction through T cell receptors: consensus, controversies and future outlooks.Experimental & molecular medicine · 2026Review
- Article
- Dynamical network analysis reveals long-range residue couplings at the pMHC interface underlying enhanced immunogenicity.NPJ systems biology and applications · 2026Article
- T-cell virtuosity in ''knowing thyself".Frontiers in immunology · 2024Review
- The Energetic Landscape of Catch Bonds in TCR Interfaces.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- The Enigmatic Nature of the TCR-pMHC Interaction: Implications for CAR-T and TCR-T Engineering.International journal of molecular sciences · 2022Review
- Structurally silent peptide anchor modifications allosterically modulate T cell recognition in a receptor-dependent manner.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Peptide-MHC Binding Reveals Conserved Allosteric Sites in MHC Class I- and Class II-Restricted T Cell Receptors (TCRs).Journal of molecular biology · 2020Article
- Tuning antiviral CD8 T-cell response via proline-altered peptide ligand vaccination.PLoS pathogens · 2020Article
- A study of CDR3 loop dynamics reveals distinct mechanisms of peptide recognition by T-cell receptors exhibiting different levels of cross-reactivity.Immunology · 2018Article
- The Hypervariable Loops of Free TCRs Sample Multiple Distinct Metastable Conformations in Solution.Frontiers in molecular biosciences · 2018Article
- The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling.Frontiers in immunology · 2018Review
- Microfluidic platform for characterizing TCR-pMHC interactions.Biomicrofluidics · 2017Article
- Exploration of the Conformational Dynamics of Major Histocompatibility Complex Molecules.Frontiers in immunology · 2017Review
- Peptide and Peptide-Dependent Motions in MHC Proteins: Immunological Implications and Biophysical Underpinnings.Frontiers in immunology · 2017Review
- The contribution of major histocompatibility complex contacts to the affinity and kinetics of T cell receptor binding.Scientific reports · 2016Article
- Hotspot autoimmune T cell receptor binding underlies pathogen and insulin peptide cross-reactivity.The Journal of clinical investigation · 2016Article
- Differential utilization of binding loop flexibility in T cell receptor ligand selection and cross-reactivity.Scientific reports · 2016Article
- A Molecular Switch Abrogates Glycoprotein 100 (gp100) T-cell Receptor (TCR) Targeting of a Human Melanoma Antigen.The Journal of biological chemistry · 2016Article
- Structure of a TCR-Mimic Antibody with Target Predicts Pharmacogenetics.Journal of molecular biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
alphabeta T-cell receptors (TCRs) recognize peptide antigens presented by class I or class II major histocompatibility complex molecules (pMHC). Here we review the use of thermodynamic measurements in the study of TCR-pMHC interactions, with attention to the diversity in binding thermodynamics and how this is related to the variation in TCR-pMHC interfaces. We show that there is no enthalpic or entropic signature for TCR binding; rather, enthalpy and entropy changes vary in a compensatory manner that reflects a narrow free energy window for the interactions that have been characterized. Binding enthalpy and entropy changes do not correlate with structural features such as buried surface area or the number of hydrogen bonds within TCR-pMHC interfaces, possibly reflecting the myriad of contributors to binding thermodynamics, but likely also reflecting a reliance on van't Hoff over calorimetric measurements and the unaccounted influence of equilibria linked to binding. TCR-pMHC binding heat capacity changes likewise vary considerably. In some cases, the heat capacity changes are consistent with conformational differences between bound and free receptors, but there is little data indicating these conformational differences represent the need to organize disordered CDR loops. In this regard, we discuss how thermodynamics may provide additional insight into conformational changes occurring upon TCR binding. Finally, we highlight opportunities for the further use of thermodynamic measurements in the study of TCR-pMHC interactions, not only for understanding TCR binding in general, but also for understanding specifics of individual interactions and the engineering of TCRs with desired molecular recognition properties.
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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.