Journal
TRENDS IN IMMUNOLOGY
Volume 34, Issue 10, Pages 495-501Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.it.2013.06.002
Keywords
antigen presentation; MHC class II molecules
Categories
Funding
- National Institutes of Health [RO1 NS044914, PO1 AI045757]
- National Multiple Sclerosis Society
- American Diabetes Association
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Recently, crystal structures of key complexes in antigen presentation have been reported. HLA-DM functions in antigen presentation by catalyzing dissociation of an invariant chain remnant from the peptide binding groove and stabilizing empty MHC class II proteins in a peptide-receptive conformation. The crystal structure of a MHC class II-HLA-DM complex explains how HLA-DM stabilizes an otherwise short-lived transition state and promotes a rapid peptide exchange process that favors the highest-affinity ligands. HLA-DO has sequence similarity with MHC class II molecules yet inhibits antigen presentation. The structure of the HLA-DO-HLA-DM complex shows that it blocks HLA-DM activity as a substrate mimic. Alterations in the efficiency of DM-mediated peptide selection may contribute to autoimmune pathologies, which will be an exciting area for future investigation.
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