3UNE
Mouse constitutive 20S proteasome
Summary for 3UNE
| Entry DOI | 10.2210/pdb3une/pdb |
| Related | 1IRU 1PMA 1RYP 3UN4 3UN8 3UNB 3UNF 3UNH |
| Descriptor | Proteasome subunit alpha type-2, Proteasome subunit beta type-2, Proteasome subunit beta type-5, ... (15 entities in total) |
| Functional Keywords | 20s proteasome comprises 28 subunits, protease, cytosol, hydrolase |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Cytoplasm: P49722 Q9R1P3 O55234 O09061 Q60692 Q9R1P0 Q9Z2U0 Q9Z2U1 Q9R1P4 O70435 Q9QUM9 P70195 Q9R1P1 Cytoplasm (By similarity): P99026 |
| Total number of polymer chains | 56 |
| Total formula weight | 1435887.89 |
| Authors | Huber, E.,Basler, M.,Schwab, R.,Heinemeyer, W.,Kirk, C.,Groettrup, M.,Groll, M. (deposition date: 2011-11-15, release date: 2012-02-29, Last modification date: 2024-11-20) |
| Primary citation | Huber, E.M.,Basler, M.,Schwab, R.,Heinemeyer, W.,Kirk, C.J.,Groettrup, M.,Groll, M. Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. Cell(Cambridge,Mass.), 148:727-738, 2012 Cited by PubMed Abstract: Constitutive proteasomes and immunoproteasomes shape the peptide repertoire presented by major histocompatibility complex class I (MHC-I) molecules by harboring different sets of catalytically active subunits. Here, we present the crystal structures of constitutive proteasomes and immunoproteasomes from mouse in the presence and absence of the epoxyketone inhibitor PR-957 (ONX 0914) at 2.9 Å resolution. Based on our X-ray data, we propose a unique catalytic feature for the immunoproteasome subunit β5i/LMP7. Comparison of ligand-free and ligand-bound proteasomes reveals conformational changes in the S1 pocket of β5c/X but not β5i, thereby explaining the selectivity of PR-957 for β5i. Time-resolved structures of yeast proteasome:PR-957 complexes indicate that ligand docking to the active site occurs only via the reactive head group and the P1 side chain. Together, our results support structure-guided design of inhibitory lead structures selective for immunoproteasomes that are linked to cytokine production and diseases like cancer and autoimmune disorders. PubMed: 22341445DOI: 10.1016/j.cell.2011.12.030 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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