ArticleScience (New York, N.Y.)2017
Structure of the TAPBPR-MHC I complex defines the mechanism of peptide loading and editing.
Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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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.
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Who cites it
77 citing papers in PubMed, 143 citations in OpenAlex.
- Reconstitution of glycan-driven MHC-I recycling reveals calreticulin as mediator between TAPBPR and tapasin.The EMBO journal · 2026Article
- Review
- Dynamic states of an MHC class I molecule during peptide exchange.Nature communications · 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
- Utilizing TAPBPR for Peptide Loading, Dissociation, and Exchange on Plasma Membrane-Expressed MHC-I.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Mouse TAPBPR shows functional similarity to human TAPBPR in shaping the MHC-I immunopeptidome.Frontiers in immunology · 2026Article
- Identification of novel HLA class I-restricted hepatitis B virus peptides and their modulation by peptide editor TAPBPR.Frontiers in immunology · 2026Article
- 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
- Evidence of focusing the MHC class I immunopeptidome by tapasin.Frontiers in immunology · 2025Article
- TAPBPR promotes editing of the HLA-B44 peptide repertoire, increasing the presentation of peptides containing a C-terminal tryptophan.Frontiers in immunology · 2025Article
- How conformational changes near the F pocket of MHC class I proteins mediate chaperone assisted peptide loading.Frontiers in immunology · 2025Article
- Review
- Review
- Reanalysis of Immunopeptidomics Datasets Provides Mechanistic Insight into TAPBPR-Mediated Peptide Editing on HLA-A, -B and -C Molecules.Wellcome open research · 2024Article
- Major histocompatibility complex class I assembly within endolysosomal pathways.Current opinion in immunology · 2023Review
- 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
- Article
- Characterization of chimeric antigen receptor modified T cells expressing scFv-IL-13Rα2 after radiolabeling withJournal of translational medicine · 2023Article
- Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes.Science advances · 2023Article
17 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adaptive immunity is shaped by a selection of peptides presented on major histocompatibility complex class I (MHC I) molecules. The chaperones Tapasin (Tsn) and TAP-binding protein-related (TAPBPR) facilitate MHC I peptide loading and high-affinity epitope selection. Despite the pivotal role of Tsn and TAPBPR in controlling the hierarchical immune response, their catalytic mechanism remains unknown. Here, we present the x-ray structure of the TAPBPR-MHC I complex, which delineates the central step of catalysis. TAPBPR functions as peptide selector by remodeling the MHC I α2-1-helix region, stabilizing the empty binding groove, and inserting a loop into the groove that interferes with peptide binding. The complex explains how mutations in MHC I-specific chaperones cause defects in antigen processing and suggests a unifying mechanism of peptide proofreading.
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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.