Journal
JOURNAL OF IMMUNOLOGY
Volume 184, Issue 3, Pages 1153-1158Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.0902878
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- National Institutes of Health [RO1AI63016]
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The mechanism by which HLA-DM (DM) promotes exchange of peptides bound to HLA-DR (DR) is still unclear. We have shown that peptide interaction with DR1 can be considered a folding process as evidenced by cooperativity. However, in DM-mediated ligand exchange, prebound peptide release is noncooperative, which could be a function of the breaking of a critical interaction. The hydrogen bond (H-bond) between beta-chain His(81) and the peptide backbone at the -1 position is a candidate for such a target. In this study, we analyze the exchange of peptides bound to a DR1. mutant in which formation of this H-bond is impaired. We observe that DM still functions normally. However, as expected of a cooperative model, this H-bond contributes to the overall energetics of the complex and its disruption impacts the ability of the exchange ligand to fold with the binding groove into a stable complex. The Journal of Immunology, 2010, 184: 1153-1158.
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