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-Structure paper
Title | Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. |
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Journal, issue, pages | Cell(Cambridge,Mass. ), Vol. 148, Page 727-738, Year 2012 |
Publish date | Nov 15, 2011 (structure data deposition date) |
![]() | Huber, E.M. / Basler, M. / Schwab, R. / Heinemeyer, W. / Kirk, C.J. / Groettrup, M. / Groll, M. |
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Methods | X-ray diffraction |
Resolution | 2.7 - 3.4 Å |
Structure data | ![]() PDB-3un4: ![]() PDB-3un8: ![]() PDB-3unb: ![]() PDB-3une: ![]() PDB-3unf: ![]() PDB-3unh: |
Chemicals | ![]() ChemComp-04C: ![]() ChemComp-HOH: ![]() ChemComp-049: ![]() ChemComp-CL: ![]() ChemComp-K: ![]() ChemComp-IOD: |
Source |
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![]() | HYDROLASE/HYDROLASE INHIBITOR / Proteasome / antigen presentation / drug development / protein degradation / HYDROLASE -HYDROLASE-INHIBITOR complex / HYDROLASE-HYDROLASE INHIBITOR complex / HYDROLASE/HYDROLASE INHIBTIOR / HYDROLASE-HYDROLASE INHIBTIOR complex / 20S proteasome comprises 28 subunits; each subunit adopts the fold of an antiparallel beta-sheet flanked by helices / Protease / Regulatory complexes / Covalent binding of PR-957 to all active sites / HYDROLASE / 20S proteasome comprises 28 subunits / Cytosol |