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Aberrant intermolecular disulfide bonding in a mutant HLA-DM molecule: implications for assembly, maturation, and

R Busch1, R C Doebele, E von Scheven

  • 1Department of Pediatrics, Stanford University Medical Center, CA 94305, USA. rbusch@leland.stanford.edu

Journal of Immunology (Baltimore, Md. : 1950)
|April 29, 1998
PubMed
Summary

A mutation in HLA-DM (DM) causes misfolding, ER retention, and degradation, impairing antigen presentation. Restoring wild-type DM function resolves these peptide-loading defects.

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