ReviewImmunologic research2013
For many but not for all: how the conformational flexibility of the peptide/MHCII complex shapes epitope selection.
Review in Immunologic research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Screening strategy for the selection of Leishmania spp. epitopes in humans through molecular interactions analysis: A bioinformatics approachBiomedica : revista del Instituto Nacional de Salud · 2026Article
- Discovery of KC-1: a novel porcine dendritic cell-targeting peptide with potential applications in swine vaccine design.BMC veterinary research · 2026Article
- A common network of residue-residue contacts underlies interactions between peptides and HLA class II complex.PloS one · 2026Article
- Non-Glycosylated SARS-CoV-2 Omicron BA.5 Receptor Binding Domain (RBD) with a Native-like Conformation Induces a Robust Immune Response with Potent Neutralization in a Mouse Model.Molecules (Basel, Switzerland) · 2024Article
- How Thymocyte Deletion in the Cortex May Curtail Antigen-Specific T-Regulatory Cell Development in the Medulla.Frontiers in immunology · 2022Article
- A Simplified Amino Acidic Alphabet to Unveil the T-Cells Receptors Antigens: A Computational Perspective.Frontiers in chemistry · 2021Article
- A Newly Recognized Pairing Mechanism of the α- and β-Chains of the Chicken Peptide-MHC Class II Complex.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Characterization of T Cells Specific for CFP-10 and ESAT-6 in Mycobacterium tuberculosis-Infected Mauritian Cynomolgus Macaques.Infection and immunity · 2017Article
- MHC class II complexes sample intermediate states along the peptide exchange pathway.Nature communications · 2016Article
- Side-Chain Conformational Preferences Govern Protein-Protein Interactions.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
The adaptive immune response starts when CD4+ T cells recognize peptide antigens presented by class II molecules of the Major Histocompatibility Complex (MHCII). Two outstanding features of MHCII molecules are their polymorphism and the ability of each allele to bind a large panoply of peptides. The ability of each MHCII molecule to interact with a limited, though broad, range of amino acid sequences, or "permissive specificity" of binding, is the result of structural flexibility. This flexibility has been identified through biochemical and biophysical studies, and molecular dynamic simulations have modeled the conformational rearrangements that the peptide and the MHCII undergo during interaction. Moreover, there is evidence that the structural flexibility of the peptide/MHCII complex correlates with the activity of the "peptide-editing" molecule DM. In light of the impact that these recent findings have on our ability to predict MHCII epitopes, a review of the structural and thermodynamic determinants of peptide binding to MHCII is proposed.
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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.