ArticleThe Journal of biological chemistry2017
Direct evidence for conformational dynamics in major histocompatibility complex class I molecules.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The trial behind it
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Who cites it
27 citing papers in PubMed, 37 citations in OpenAlex.
- Genetic characterization of the TAPBP and its allelic association with BF2 in the chicken major histocompatibility complex.Immunogenetics · 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
- Identification and biophysical characterization of Plasmodium peptide binding by common African HLAs.Scientific reports · 2025Article
- CryoEM structure of an MHC-I/TAPBPR peptide-bound intermediate reveals the mechanism of antigen proofreading.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Quantifying conformational changes in the TCR:pMHC-I binding interface.Frontiers in immunology · 2024Article
- Structure, function, and immunomodulation of the CD8 co-receptor.Frontiers in immunology · 2024Review
- 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
- Visualising tapasin- and TAPBPR-assisted editing of major histocompatibility complex class-I immunopeptidomes.Current opinion in immunology · 2023Review
- Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes.Science advances · 2023Article
- Unusual crystal structures of MHC class I complexes reveal the elusive intermediate conformations explored during peptide editing in antigen presentation.Research square · 2023Article
- Partial peptide dissociation and binding groove plasticity in two major histocompatibility complex class I alleles - differences between allelesRSC advances · 2022Article
- Peptide-dependent tuning of major histocompatibility complex motional properties and the consequences for cellular immunity.Current opinion in immunology · 2022Review
- TCR-pMHC: Envisioning the specialized dynamics of the target 5-component complex.Cellular & molecular immunology · 2022Article
- Is There a Need for a More Precise Description of Biomolecule Interactions to Understand Cell Function?Current issues in molecular biology · 2022Review
- Dynamics of MHC-I molecules in the antigen processing and presentation pathway.Current opinion in immunology · 2021Review
- Kinetics of Abacavir-Induced Remodelling of the Major Histocompatibility Complex Class I Peptide Repertoire.Frontiers in immunology · 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
- Atomistic structure and dynamics of the human MHC-I peptide-loading complex.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Major histocompatibility complex class I molecules (MHC I) help protect jawed vertebrates by binding and presenting immunogenic peptides to cytotoxic T lymphocytes. Peptides are selected from a large diversity present in the endoplasmic reticulum. However, only a limited number of peptides complement the polymorphic MHC specificity determining pockets in a way that leads to high-affinity peptide binding and efficient antigen presentation. MHC I molecules possess an intrinsic ability to discriminate between peptides, which varies in efficiency between allotypes, but the mechanism of selection is unknown. Elucidation of the selection mechanism is likely to benefit future immune-modulatory therapies. Evidence suggests peptide selection involves transient adoption of alternative, presumably higher energy conformations than native peptide-MHC complexes. However, the instability of peptide-receptive MHC molecules has hindered characterization of such conformational plasticity. To investigate the dynamic nature of MHC, we refolded MHC proteins with peptides that can be hydrolyzed by UV light and thus released. We compared the resultant peptide-receptive MHC molecules with non-hydrolyzed peptide-loaded MHC complexes by monitoring the exchange of hydrogen for deuterium in solution. We found differences in hydrogen-deuterium exchange between peptide-loaded and peptide-receptive molecules that were negated by the addition of peptide to peptide-receptive MHC molecules. Peptide hydrolysis caused significant increases in hydrogen-deuterium exchange in sub-regions of the peptide-binding domain and smaller increases elsewhere, including in the α3 domain and the non-covalently associated β
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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.