The kinetic basis of peptide exchange catalysis by HLA-DM

Proceedings of the National Academy of Sciences of the United States of America
J A ZarutskieLawrence J Stern

Abstract

The mechanism by which the peptide exchange factor HLA-DM catalyzes peptide loading onto structurally homologous class II MHC proteins is an outstanding problem in antigen presentation. The peptide-loading reaction of class II MHC proteins is complex and includes conformational changes in both empty and peptide-bound forms in addition to a bimolecular binding step. By using a fluorescence energy transfer assay to follow the kinetics of peptide binding to the human class II MHC protein HLA-DR1, we find that HLA-DM catalyzes peptide exchange by facilitating a conformational change in the peptide-bound complex, and not by promoting the bimolecular MHC-peptide reaction or the conversion between peptide-receptive and -averse forms of the empty protein. Thus, HLA-DM serves essentially as a protein-folding or conformational catalyst.

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Citations

May 16, 2002·Journal of Immunological Methods·Robert BuschElizabeth D Mellins
Sep 8, 2012·Nature Reviews. Immunology·James F Mohan, Emil R Unanue
Dec 12, 2012·Nature Structural & Molecular Biology·Abigail I GuceLawrence J Stern
Nov 16, 2011·Proceedings of the National Academy of Sciences of the United States of America·Corrie A PainterLawrence J Stern
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Apr 23, 2003·The Journal of Immunology : Official Journal of the American Association of Immunologists·Robert C DoebeleElizabeth D Mellins

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