Summary for 3E47
Entry DOI | 10.2210/pdb3e47/pdb |
Related | 1ryp |
Descriptor | Proteasome component Y7, Proteasome component C11, Proteasome component PRE2, ... (16 entities in total) |
Functional Keywords | proteasome, ubiquitin, protein degradation, inhibitor, immunology, cytoplasm, hydrolase, nucleus, phosphoprotein, protease, threonine protease, ubl conjugation, zymogen |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Cellular location | Cytoplasm: P23639 P22141 P30656 P23724 P30657 P38624 P23638 P40303 P32379 P40302 P21242 P21243 P25043 P25451 |
Total number of polymer chains | 28 |
Total formula weight | 705401.64 |
Authors | Groll, M.,Larionov, O.V.,de Meijere, A. (deposition date: 2008-08-10, release date: 2008-09-02, Last modification date: 2024-10-09) |
Primary citation | Groll, M.,Larionov, O.V.,Huber, R.,de Meijere, A. Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation Proc.Natl.Acad.Sci.Usa, 103:4576-4579, 2006 Cited by PubMed 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-gamma 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. PubMed: 16537370DOI: 10.1073/pnas.0600647103 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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