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• W1980712927 abstract "Most class I MHC ligands are generated from the vast majority of cellular proteins by proteolysis within the ubiquitin–proteasome pathway and are presented on the cell surface by MHC class I molecules. Here, we present the crystallographic analysis of yeast 20S proteasome in complex with the inhibitor homobelactosin C. The structure reveals a unique inhibitor-binding mode and provides information about the composition of proteasomal primed substrate-binding sites. IFN-γ inducible substitution of proteasomal constitutive subunits by immunosubunits modulates characteristics of generated peptides, thus producing fragments with higher preference for binding to MHC class I molecules. The structural data for the proteasome:homobelactosin C complex provide an explanation for involvement of immunosubunits in antigen generation and open perspectives for rational design of ligands, inhibiting exclusively constitutive proteasomes or immunoproteasomes." @default.
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• W1980712927 date "2006-03-13" @default.
• W1980712927 modified "2023-10-16" @default.
• W1980712927 title "Inhibitor-binding mode of homobelactosin C to proteasomes: New insights into class I MHC ligand generation" @default.
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• W1980712927 doi "https://doi.org/10.1073/pnas.0600647103" @default.
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