Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3E47

Crystal Structure of the Yeast 20S Proteasome in Complex with Homobelactosin C

Replaces:  2FNY
Summary for 3E47
Entry DOI10.2210/pdb3e47/pdb
Related1ryp
DescriptorProteasome component Y7, Proteasome component C11, Proteasome component PRE2, ... (16 entities in total)
Functional Keywordsproteasome, ubiquitin, protein degradation, inhibitor, immunology, cytoplasm, hydrolase, nucleus, phosphoprotein, protease, threonine protease, ubl conjugation, zymogen
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Cellular locationCytoplasm: P23639 P22141 P30656 P23724 P30657 P38624 P23638 P40303 P32379 P40302 P21242 P21243 P25043 P25451
Total number of polymer chains28
Total formula weight705401.64
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 citationGroll, 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: 16537370
DOI: 10.1073/pnas.0600647103
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

227111

数据于2024-11-06公开中

PDB statisticsPDBj update infoContact PDBjnumon