منابع مشابه
Antigen processing: HLA-DO – a hitchhiking inhibitor of HLA-DM
Recent studies have revealed that the conserved major histocompatibility complex class II molecule, HLA-DO, inhibits the class II antigen-processing pathway. HLA-DO, expressed in only a subset of antigen-presenting cells, binds HLA-DM and blocks HLA-DM-catalyzed peptide loading of class II molecules.
متن کاملTransmembrane domain-mediated colocalization of HLA-DM and HLA-DR is required for optimal HLA-DM catalytic activity.
HLA-DM catalyzes peptide loading and exchange reactions by MHC class II molecules. Soluble recombinant DM, lacking transmembrane and cytoplasmic domains, was observed to have 200- to 400-fold less activity compared with the full-length protein in assays measuring DM-catalyzed peptide dissociation from purified HLA-DR1 in detergent solutions. Additional studies with truncated soluble DR1 demonst...
متن کاملShort peptide sequences mimic HLA-DM functions.
HLA-DM (DM) plays a critical role in Ag presentation to CD4 T cells by catalyzing the exchange of peptides bound to MHC class II molecules. It is known that DM interaction with MHC II involves conformational changes in the MHC II molecule leading to the disturbance of H-bonds formed between the bound peptide and the MHC II groove leading to peptide dissociation. The specific region of the DM mo...
متن کاملHLA-DP, HLA-DQ, and HLA-DR have different requirements for invariant chain and HLA-DM.
The MHC is central to the adaptive immune response. The human MHC class II is encoded by three different isotypes, HLA-DR, -DQ, and -DP, each being highly polymorphic. In contrast to HLA-DR, the intracellular assembly and trafficking of HLA-DP molecules have not been studied extensively. However, different HLA-DP variants can be either protective or risk factors for infectious diseases (e.g. he...
متن کاملHLA-DM Interactions with Intermediates in HLA-DR Maturation and a Role for HLA-DM in Stabilizing Empty HLA-DR Molecules
Major histocompatibility complex (MHC) class II-positive cell lines which lack HLA-DM expression accumulate class II molecules associated with residual invariant (I) chain fragments (class II-associated invariant chain peptides [CLIP]). In vitro, HLA-DM catalyzes CLIP dissociation from class II-CLIP complexes, promoting binding of antigenic peptides. Here the physical interaction of HLA-DM with...
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ژورنال
عنوان ژورنال: Immunology
سال: 2013
ISSN: 0019-2805
DOI: 10.1111/imm.12030