4r18

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'''Unreleased structure'''
 
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The entry 4r18 is ON HOLD
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==Ligand-induced Lys33-Thr1 crosslinking at subunit beta5 of the yeast 20S proteasome==
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<StructureSection load='4r18' size='340' side='right'caption='[[4r18]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4r18]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R18 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4r18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r18 OCA], [https://pdbe.org/4r18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r18 RCSB], [https://www.ebi.ac.uk/pdbsum/4r18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r18 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PSA6_YEAST PSA6_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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The concept of proteasome inhibition ranks among the latest achievements in the treatment of blood cancer and represents a promising strategy for modulating autoimmune diseases. In this study, we describe peptidic sulfonyl fluoride inhibitors that selectively block the catalytic beta5 subunit of the immunoproteasome by inducing only marginal cytotoxic effects. Structural and mass spectrometric analyses revealed a novel reaction mechanism involving polarity inversion and irreversible crosslinking of the proteasomal active site. We thus identified the sulfonyl fluoride headgroup for the development and optimization of immunoproteasome selective compounds and their possible application in autoimmune disorders.
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Authors: Dubiella, C., Cui, H., Gersch, M., Brouwer, A. J., Sieber, S. A., Krueger, A., Liskamp, R. M. J., Groll, M.
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Selective Inhibition of the Immunoproteasome by Ligand-Induced Crosslinking of the Active Site.,Dubiella C, Cui H, Gersch M, Brouwer AJ, Sieber SA, Kruger A, Liskamp RM, Groll M Angew Chem Int Ed Engl. 2014 Sep 22. doi: 10.1002/anie.201406964. PMID:25244435<ref>PMID:25244435</ref>
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Description: Ligand-induced Lys33-Thr1 crosslinking at subunit beta5 of the yeast 20S proteasome
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4r18" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Proteasome 3D structures|Proteasome 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Brouwer AJ]]
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[[Category: Cui H]]
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[[Category: Dubiella C]]
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[[Category: Gersch M]]
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[[Category: Groll M]]
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[[Category: Krueger A]]
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[[Category: Liskamp R]]
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[[Category: Sieber SA]]

Current revision

Ligand-induced Lys33-Thr1 crosslinking at subunit beta5 of the yeast 20S proteasome

PDB ID 4r18

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