3okj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Alpha-keto-aldehyde binding mechanism reveals a novel lead structure motif for proteasome inhibition== | |
| + | <StructureSection load='3okj' size='340' side='right'caption='[[3okj]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3okj]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OKJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP9:N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-[(2S,3S)-3-HYDROXY-1-(4-HYDROXYPHENYL)-4-OXOBUTAN-2-YL]-L-LEUCINAMIDE'>EP9</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=3okj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3okj OCA], [https://pdbe.org/3okj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3okj RCSB], [https://www.ebi.ac.uk/pdbsum/3okj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3okj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PSA2_YEAST PSA2_YEAST] The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that 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. It has an ATP-dependent proteolytic activity. | ||
| - | + | ==See Also== | |
| - | + | *[[Proteasome 3D structures|Proteasome 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Gallastegui P]] | ||
| + | [[Category: Groll M]] | ||
| + | [[Category: Huber R]] | ||
| + | [[Category: Kloetzel PM]] | ||
| + | [[Category: Poynor M]] | ||
| + | [[Category: Schmidt B]] | ||
| + | [[Category: Stein M]] | ||
Current revision
Alpha-keto-aldehyde binding mechanism reveals a novel lead structure motif for proteasome inhibition
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