Abstract
Assembly of functional major histocompatibility complex (MHC) class I peptide complexes within the endoplasmic reticulum is critically important for the development of an adaptive immune response. The highly regulated loading of peptides onto MHC class I molecules is controlled by a multi-component chaperone system called the MHC class I peptide loading complex. The recent identification of the thioredoxin family member ERp57 as a component of the loading complex led to an interesting question: Why is there a thiol-disulfide oxidoreductase inside a complex dedicated to inserting peptides into a receptor binding site? Most recently, specific ERp57-mediated disulfide bond rearrangements have been identified inside the loading complex. What these biochemical events mean for the peptide loading process remains a matter of conjecture. While several important questions wait to be answered, this review intends to summarize our current view of the oxidative folding of MHC class I molecules and addresses the question of how the receptor ligand interaction might be regulated by thiol-based redox reactions.
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Received 8 July 2003; received after revision 19 August 2003; accepted 26 August 2003
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Dick, T.B. Assembly of MHC class I peptide complexes from the perspective of disulfide bond formation. CMLS, Cell. Mol. Life Sci. 61, 547–556 (2004). https://doi.org/10.1007/s00018-003-3271-9
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DOI: https://doi.org/10.1007/s00018-003-3271-9