Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules.

@article{Anderson1992InvariantCC,
  title={Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules.},
  author={Mark S. Anderson and Jim Miller},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1992},
  volume={89 6},
  pages={2282-6}
}
During biosynthesis, class II major histocompatibility complex molecules are intimately associated with invariant chain (Ii). The Ii-class II association has been shown to block peptide-class II binding and to affect the ultimate conformation of class II expressed on the cell surface. To assess the biochemical basis for the effects of Ii on class II, we have analyzed the biosynthesis of class II in EL4 cells transfected with I-Ad with and without Ii. In these studies, we found that Ii had a… CONTINUE READING

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