ArticleThe Journal of biological chemistry2013
Peptide modulation of class I major histocompatibility complex protein molecular flexibility and the implications for immune recognition.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 53 citations in OpenAlex.
- HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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
- Solution mapping of MHC-I:TCR interactions using a minimalistic protein system.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Evolving T Cell Receptor Recognition Code: The Rules Are More Like Guidelines.Immunological reviews · 2025Review
- Quantifying conformational changes in the TCR:pMHC-I binding interface.Frontiers in immunology · 2024Article
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- Crystal structures of MHC class I complexes reveal the elusive intermediate conformations explored during peptide editing.Nature communications · 2023Article
- Unusual crystal structures of MHC class I complexes reveal the elusive intermediate conformations explored during peptide editing in antigen presentation.Research square · 2023Article
- Conformational flexibility of a free and TCR-bound pMHC-I protein investigated by long-term molecular dynamics simulations.BMC immunology · 2022Article
- Primary and secondary functions of HLA-E are determined by stability and conformation of the peptide-bound complexes.Cell reports · 2022Article
- Peptide-dependent tuning of major histocompatibility complex motional properties and the consequences for cellular immunity.Current opinion in immunology · 2022Review
- Dynamics of MHC-I molecules in the antigen processing and presentation pathway.Current opinion in immunology · 2021Review
- 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
- Markov state modeling reveals alternative unbinding pathways for peptide-MHC complexes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- 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
- Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Dynamically Driven Allostery in MHC Proteins: Peptide-Dependent Tuning of Class I MHC Global Flexibility.Frontiers in immunology · 2019Article
- The intersection of affinity and specificity in the development and optimization of T cell receptor based therapeutics.Seminars in cell & developmental biology · 2018Review
- General Prediction of Peptide-MHC Binding Modes Using Incremental Docking: A Proof of Concept.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
T cells use the αβ T cell receptor (TCR) to recognize antigenic peptides presented by class I major histocompatibility complex proteins (pMHCs) on the surfaces of antigen-presenting cells. Flexibility in both TCRs and peptides plays an important role in antigen recognition and discrimination. Less clear is the role of flexibility in the MHC protein; although recent observations have indicated that mobility in the MHC can impact TCR recognition in a peptide-dependent fashion, the extent of this behavior is unknown. Here, using hydrogen/deuterium exchange, fluorescence anisotropy, and structural analyses, we show that the flexibility of the peptide binding groove of the class I MHC protein HLA-A*0201 varies significantly with different peptides. The variations extend throughout the binding groove, impacting regions contacted by TCRs as well as other activating and inhibitory receptors of the immune system. Our results are consistent with statistical mechanical models of protein structure and dynamics, in which the binding of different peptides alters the populations and exchange kinetics of substates in the MHC conformational ensemble. Altered MHC flexibility will influence receptor engagement, impacting conformational adaptations, entropic penalties associated with receptor recognition, and the populations of binding-competent states. Our results highlight a previously unrecognized aspect of the "altered self" mechanism of immune recognition and have implications for specificity, cross-reactivity, and antigenicity in cellular immunity.
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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.