Chaperone-mediated MHC-I peptide exchange in antigen presentation

This topic review summarizes structures of chaperones complexed with MHC-I, the structural principles that govern peptide exchange and the mechanism in antigen presentation.

• Publication year

  2024

• Venue

  IUCrJ

• Publication date

  2024-04-24

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1107/S2052252524002768PMID 38656309PMCID 11067752
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Chaperone function in antigen presentation by MHC class I molecules—tapasin in the PLC and TAPBPR beyond

  2023cited by this paper
• Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes

  2023cited by this paper
• Get into the groove! The influence of TAPBPR on cargo selection.

  2023cited by this paper
• Visualising tapasin- and TAPBPR-assisted editing of major histocompatibility complex class-I immunopeptidomes

  2023cited by this paper
• Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes

  2023cited by this paper
• The mode of action of tapasin on major histocompatibility class I (MHC-I) molecules

  2023cited by this paper
• Advancing our knowledge of antigen processing with computational modelling, structural biology, and immunology.

  2023cited by this paper
• Mass Spectrometric Profiling of HLA-B44 Peptidomes Provides Evidence for Tapasin-Mediated Tryptophan Editing.

  2023cited by this paper
• Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity

  2022cited by this paper
• Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation

  2022cited by this paper
• The IPD-IMGT/HLA Database

  2022cited by this paper
• Structure of an MHC I–tapasin–ERp57 editing complex defines chaperone promiscuity

  2022cited by this paper
• Molecular basis of MHC I quality control in the peptide loading complex

  2022cited by this paper
• A guide to antigen processing and presentation

  2022cited by this paper
• Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules

  2021cited by this paper
• 50 Years of structural immunology

  2021cited by this paper
• A loop structure allows TAPBPR to exert its dual function as MHC I chaperone and peptide editor

  2020cited by this paper
• UCSF ChimeraX: Structure visualization for researchers, educators, and developers

  2020cited by this paper
• The susceptibility of disulfide bonds towards radiation damage may be explained by S⋯O interactions

  2020cited by this paper
• Atomistic structure and dynamics of the human MHC-I peptide-loading complex

  2020cited by this paper
• Structural and dynamic studies of TAPBPR and Tapasin reveal the mechanism of peptide loading of MHC-I molecules.

  2020cited by this paper
• TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap

  2020cited by this paper
• Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection

  2020cited by this paper
• Nomenclature for factors of the HLA system, update July, August and September 2019

  2019cited by this paper
• MHC-I peptide binding activity assessed by exchange after cleavage of peptide covalently linked to β2-microglobulin.

  2019cited by this paper
• Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway

  2019cited by this paper
• A large peptidome dataset improves HLA class I epitope prediction across most of the human population

  2019cited by this paper
• MHC Molecules, T cell Receptors, Natural Killer Cell Receptors, and Viral Immunoevasins-Key Elements of Adaptive and Innate Immunity.

  2019cited by this paper
• TAPBPR mediates peptide dissociation from MHC class I using a leucine lever

  2018cited by this paper
• The N-terminal region of photocleavable peptides that bind HLA-DR1 determines the kinetics of fragment release

  2018cited by this paper
• The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling

  2018cited by this paper
• Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle

  2018cited by this paper
• The Immune Epitope Database (IEDB): 2018 update

  2018cited by this paper
• Crystal structure of a TAPBPR–MHC I complex reveals the mechanism of peptide editing in antigen presentation

  2017cited by this paper
• Structure of the TAPBPR–MHC I complex defines the mechanism of peptide loading and editing

  2017cited by this paper
• Structure of the human MHC-I peptide-loading complex

  2017cited by this paper
• Present Yourself! By MHC Class I and MHC Class II Molecules.

  2016cited by this paper
• Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing

  2016cited by this paper
• Molecular mechanism of peptide editing in the tapasin–MHC I complex

  2016cited by this paper
• TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst

  2015cited by this paper
• HLA-DM and HLA-DO, key regulators of MHC-II processing and presentation.

  2014cited by this paper
• Invariant chain–MHC class II complexes: always odd and never invariant

  2014cited by this paper
• Analysis of Relationships between Peptide/MHC Structural Features and Naive T Cell Frequency in Humans

  2014cited by this paper
• Pathways of antigen processing.

  2013cited by this paper
• Dipeptides promote folding and peptide binding of MHC class I molecules

  2013cited by this paper
• Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathway

  2013cited by this paper
• HLA-DO acts as a substrate mimic to inhibit HLA-DM by a competitive mechanism

  2012cited by this paper
• Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection.

  2012cited by this paper
• Invariant chain increases the half‐life of MHC II by delaying endosomal maturation

  2011cited by this paper
• UV-induced ligand exchange in MHC class I protein crystals.

  2009cited by this paper
• Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer.

  2009cited by this paper
• The structure of HLA-DR52c: Comparison to other HLA-DRB3 alleles

  2008cited by this paper
• Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection

  2007cited by this paper
• Direct peptide-regulatable interactions between MHC class I molecules and tapasin

  2006cited by this paper
• Design and use of conditional MHC class I ligands

  2006cited by this paper
• IMGT/3Dstructure-DB and IMGT/StructuralQuery, a database and a tool for immunoglobulin, T cell receptor and MHC structural data

  2004cited by this paper
• A human TAPBP (TAPASIN)‐related gene, TAPBP‐R

  2002cited by this paper
• Specific chemical and structural damage to proteins produced by synchrotron radiation.

  2000cited by this paper
• IMGT, the international ImMunoGeneTics database

  1999cited by this paper
• Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution.

  1991cited by this paper
• Antibody structure and molecular immunology.

  1973cited by this paper
• The structure of the heavy chain of immunoglobulin and its relevance to the nature of the antibody-combining site. The Second CIBA Medal Lecture.

  1967cited by this paper
• AN ELECTROPHORETIC STUDY OF IMMUNE SERA AND PURIFIED ANTIBODY PREPARATIONS

  1939cited by this paper

• Fish CD8+ T cells: Current knowledge and research perspectives

  2026cites this paper
• CryoEM structure of an MHC-I/TAPBPR peptide-bound intermediate reveals the mechanism of antigen proofreading

  2025cites this paper
• The potential applications of peptide-loading complex in cancer treatment

  2025cites this paper
• CryoEM structure of an MHC-I/TAPBPR peptide bound intermediate reveals the mechanism of antigen proofreading

  2024cites this paper