Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association.

@article{Grotenbreg2007EmptyCI,
  title={Empty class II major histocompatibility complex created by peptide photolysis establishes the role of DM in peptide association.},
  author={Gijsbert M. Grotenbreg and Melissa J Nicholson and Kevin D. Fowler and Kathrin Wilbuer and Leah M. Octavio and Maxine Yang and Arup K. Chakraborty and Hidde L. Ploegh and Kai W Wucherpfennig},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 29},
  pages={21425-36}
}
DM catalyzes the exchange of peptides bound to Class II major histocompatibility complex (MHC) molecules. Because the dissociation and association components of the overall reaction are difficult to separate, a detailed mechanism of DM catalysis has long resisted elucidation. UV irradiation of DR molecules loaded with a photocleavable peptide (caged Class II MHC molecules) enabled synchronous and verifiable evacuation of the peptide-binding groove and tracking of early binding events in real… CONTINUE READING