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    HLA-DO acts as a substrate mimic to inhibit HLA-DM by a competitive mechanism

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    Authors
    Guce, Abigail I.
    Mortimer, Sarah E.
    Yoon, Taejin
    Painter, Corrie A.
    Jiang, Wei
    Mellins, Elizabeth D.
    Stern, Lawrence J.
    UMass Chan Affiliations
    Department of Pathology
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2013-01-01
    Keywords
    Animals
    Antigen Presentation
    Antigen-Presenting Cells
    Binding Sites
    Cell Line
    Crystallography, X-Ray
    Drosophila melanogaster
    HLA-D Antigens
    Humans
    Molecular Chaperones
    Mutation
    Protein Conformation
    Immunopathology
    Molecular Biology
    Structural Biology
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    Link to Full Text
    http://dx.doi.org/10.1038/nsmb.2460
    Abstract
    Mammalian class II major histocompatibility (MHCII) proteins bind peptide antigens in endosomal compartments of antigen-presenting cells. The nonclassical MHCII protein HLA-DM chaperones peptide-free MHCII, protecting it against inactivation, and catalyzes peptide exchange on loaded MHCII. Another nonclassical MHCII protein, HLA-DO, binds HLA-DM and influences the repertoire of peptides presented by MHCII proteins. However, the mechanism by which HLA-DO functions is unclear. Here we have used X-ray crystallography, enzyme kinetics and mutagenesis approaches to investigate human HLA-DO structure and function. In complex with HLA-DM, HLA-DO adopts a classical MHCII structure, with alterations near the alpha subunit's 3(1)(0) helix. HLA-DO binds to HLA-DM at the same sites implicated in MHCII interaction, and kinetic analysis showed that HLA-DO acts as a competitive inhibitor. These results show that HLA-DO inhibits HLA-DM function by acting as a substrate mimic, and the findings also limit the possible functional roles for HLA-DO in antigen presentation.
    Source
    Nat Struct Mol Biol. 2013 Jan;20(1):90-8. doi: 10.1038/nsmb.2460. Link to article on publisher's site
    DOI
    10.1038/nsmb.2460
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/30008
    PubMed ID
    23222639
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1038/nsmb.2460
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    UMass Chan Faculty and Researcher Publications

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