The complex route to MHC class I-peptide complexes

Cell. 2006 Oct 20;127(2):249-51. doi: 10.1016/j.cell.2006.10.001.

Abstract

The loading of peptides into the groove of MHC class I molecules prior to antigen presentation is a complex process. In this issue of Cell, Park et al. (2006) show that peptide loading gets a helping hand from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidoreductase activity.

Publication types

  • Comment

MeSH terms

  • Antigen Presentation*
  • Cytomegalovirus Infections / immunology
  • Cytomegalovirus Infections / metabolism
  • Histocompatibility Antigens Class I / immunology
  • Histocompatibility Antigens Class I / metabolism*
  • Humans
  • Oxidation-Reduction
  • Peptides / immunology
  • Peptides / metabolism*
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Disulfide-Isomerases / metabolism*
  • Sulfhydryl Compounds / metabolism

Substances

  • Histocompatibility Antigens Class I
  • Peptides
  • Sulfhydryl Compounds
  • Proteasome Endopeptidase Complex
  • Protein Disulfide-Isomerases