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| <StructureSection load='3unb' size='340' side='right'caption='[[3unb]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3unb' size='340' side='right'caption='[[3unb]], [[Resolution|resolution]] 2.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3unb]] is a 56 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNB FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3unb]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNB FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=04C:1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL'>04C</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pma|1pma]], [[1ryp|1ryp]], [[1iru|1iru]], [[3un8|3un8]], [[3un4|3un4]], [[3unh|3unh]], [[3unf|3unf]], [[3une|3une]]</div></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=04C:1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL'>04C</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3unb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unb OCA], [https://pdbe.org/3unb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unb RCSB], [https://www.ebi.ac.uk/pdbsum/3unb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unb ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3unb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unb OCA], [https://pdbe.org/3unb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unb RCSB], [https://www.ebi.ac.uk/pdbsum/3unb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unb ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/PSA3_MOUSE PSA3_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. [[https://www.uniprot.org/uniprot/PSB5_MOUSE PSB5_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib (By similarity). Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway.<ref>PMID:19183883</ref> [[https://www.uniprot.org/uniprot/PSA7_MOUSE PSA7_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions (By similarity). The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions (By similarity). Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response (By similarity). [[https://www.uniprot.org/uniprot/PSA6_MOUSE PSA6_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. [[https://www.uniprot.org/uniprot/PSB3_MOUSE PSB3_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. [[https://www.uniprot.org/uniprot/PSA4_MOUSE PSA4_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. [[https://www.uniprot.org/uniprot/PSB1_MOUSE PSB1_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. [[https://www.uniprot.org/uniprot/PSB6_MOUSE PSB6_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. May catalyze basal processing of intracellular antigens. [[https://www.uniprot.org/uniprot/PSB7_MOUSE PSB7_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the trypsin-like activity of the proteasome (By similarity). [[https://www.uniprot.org/uniprot/PSA2_MOUSE PSA2_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation. [[https://www.uniprot.org/uniprot/PSA5_MOUSE PSA5_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. [[https://www.uniprot.org/uniprot/PSB2_MOUSE PSB2_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit has a chymotrypsin-like activity. [[https://www.uniprot.org/uniprot/PSB4_MOUSE PSB4_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal macrophage proteasome. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By similarity).<ref>PMID:12874245</ref> [[https://www.uniprot.org/uniprot/PSA1_MOUSE PSA1_MOUSE]] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal macrophage proteasome. Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells.<ref>PMID:12874245</ref> <ref>PMID:19526544</ref>
| | [https://www.uniprot.org/uniprot/PSB7_MOUSE PSB7_MOUSE] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the trypsin-like activity of the proteasome (By similarity). |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| [[Category: Proteasome endopeptidase complex]]
| | [[Category: Basler M]] |
| [[Category: Basler, M]] | | [[Category: Groettrup M]] |
| [[Category: Groettrup, M]] | | [[Category: Groll M]] |
| [[Category: Groll, M]] | | [[Category: Heinemeyer W]] |
| [[Category: Heinemeyer, W]] | | [[Category: Huber E]] |
| [[Category: Huber, E]] | | [[Category: Kirk C]] |
| [[Category: Kirk, C]] | | [[Category: Schwab R]] |
| [[Category: Schwab, R]] | |
| [[Category: 20s proteasome comprises 28 subunit]]
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| [[Category: Covalent binding of pr-957 to all active site]]
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| [[Category: Each subunit adopts the fold of an antiparallel beta-sheet flanked by helice]]
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| [[Category: Hydrolase-hydrolase inhibitor complex]]
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| [[Category: Protease]]
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| [[Category: Regulatory complex]]
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