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pubmed-article:7596415pubmed:abstractTextHuman leukocyte antigen (HLA)-DM is an unconventional major histocompatibility complex (MHC) class II heterodimer that is important for B-cell-mediated antigen processing and presentation to MHC class II-restricted T cells. HLA-DM is encoded by two genes, DMA and DMB, which map to the MHC class II region, and shares some homology with MHC class I and class II proteins. Here we define the biochemical role of HLA-DM. Recombinant soluble HLA-DM heterodimers have been purified from culture supernatants of insect cell transformants. At pH 5.0, they induce the dissociation of a subset of peptides bound to HLA-DR, including a nested set of class-II-associated invariant chain peptides (CLIP). This process liberates HLA-DR and leads to the enhanced binding of exogenous peptides.lld:pubmed
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pubmed-article:7596415pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:7596415pubmed:articleTitleMediation by HLA-DM of dissociation of peptides from HLA-DR.lld:pubmed
pubmed-article:7596415pubmed:affiliationDepartment of Autoimmune Disease Research, Merck Research Laboratories, Rahway, New Jersey 07065, USA.lld:pubmed
pubmed-article:7596415pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7596415pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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