5a0q: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a0q]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[5a0q]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0Q FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KNM:ADA-(AHX)3-(LEU)3-VINYL+SULFONE'>KNM</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KNM:ADA-(AHX)3-(LEU)3-VINYL+SULFONE'>KNM</scene></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=5a0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0q OCA], [https://pdbe.org/5a0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0q RCSB], [https://www.ebi.ac.uk/pdbsum/5a0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0q 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=5a0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0q OCA], [https://pdbe.org/5a0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0q RCSB], [https://www.ebi.ac.uk/pdbsum/5a0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/PSA3_HUMAN PSA3_HUMAN] 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. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.<ref>PMID:11350925</ref> <ref>PMID:17499743</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Latest revision as of 14:36, 6 November 2024
Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome coreCryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core
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