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| {{Large structure}}
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| ==Mouse 20S immunoproteasome== | | ==Mouse 20S immunoproteasome== |
| <StructureSection load='3unh' size='340' side='right' caption='[[3unh]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='3unh' size='340' side='right'caption='[[3unh]], [[Resolution|resolution]] 3.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3unh]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UNH FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3unh]] is a 20 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=3UNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNH FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 3.2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pma|1pma]], [[1ryp|1ryp]], [[1iru|1iru]], [[3un4|3un4]], [[3un8|3un8]], [[3unb|3unb]], [[3une|3une]], [[3unf|3unf]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=3unh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unh OCA], [https://pdbe.org/3unh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unh RCSB], [https://www.ebi.ac.uk/pdbsum/3unh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unh ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3unh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unh OCA], [http://pdbe.org/3unh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3unh RCSB], [http://www.ebi.ac.uk/pdbsum/3unh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3unh ProSAT]</span></td></tr> | |
| </table> | | </table> |
| {{Large structure}}
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| == Function == | | == Function == |
| [[http://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. [[http://www.uniprot.org/uniprot/PSB8_MOUSE PSB8_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 is involved in antigen processing to generate class I binding peptides. May be involved in the inflammatory response pathway. Required for adipocyte differentiation.<ref>PMID:21881205</ref> <ref>PMID:22341445</ref> <ref>PMID:8066463</ref> [[http://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). [[http://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. [[http://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. [[http://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. [[http://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. [[http://www.uniprot.org/uniprot/PSB9_MOUSE PSB9_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 is involved in antigen processing to generate class I binding peptides. Contributes to NFKBIA degradation and subsequently NFKB1 generation.<ref>PMID:16222703</ref> <ref>PMID:22341445</ref> [[http://www.uniprot.org/uniprot/PSB10_MOUSE PSB10_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 is involved in antigen processing to generate class I binding peptides. Plays a role in determining the T-cell repertoire for an antiviral T-cell response.<ref>PMID:22341445</ref> [[http://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. [[http://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. [[http://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. [[http://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> [[http://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/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. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
| *[[Proteasome|Proteasome]] | | *[[Proteasome 3D structures|Proteasome 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| | [[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: Cytosol]]
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| [[Category: Hydrolase]]
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| [[Category: Protease]]
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