Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes

@article{Brown1991StructuralAS,
  title={Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes},
  author={Michael G Brown and James N. Driscoll and John J. Monaco},
  journal={Nature},
  year={1991},
  volume={353},
  pages={355-357}
}
MAJOR histocompatibility complex (MHC) class I molecules associate with peptides derived from endogenously synthesized antigens. Cytotoxic T-lymphocytes can thus scan class I molecules and bound peptide on the surface of cells for foreign antigenic determinants. Recent evidence1,2 demonstrates that the products of trans-acting, non-class I genes in the class II region of the MHC are required in the class I antigen-processing pathway. There are genes (called HAM1 and HAM2 in the mouse) in this… CONTINUE READING

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