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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4nnw]] 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=4NNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NNW FirstGlance]. <br>
<table><tr><td colspan='2'>[[4nnw]] 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=4NNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NNW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MK:N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-[(2R,3S)-1,2-DIHYDROXY-5-METHYLHEXAN-3-YL]-L-LEUCINAMIDE'>2MK</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MK:N-[(BENZYLOXY)CARBONYL]-L-LEUCYL-N-[(2R,3S)-1,2-DIHYDROXY-5-METHYLHEXAN-3-YL]-L-LEUCINAMIDE'>2MK</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4nnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnw OCA], [https://pdbe.org/4nnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nnw RCSB], [https://www.ebi.ac.uk/pdbsum/4nnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnw 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=4nnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnw OCA], [https://pdbe.org/4nnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nnw RCSB], [https://www.ebi.ac.uk/pdbsum/4nnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ubiquitin-proteasome system (UPS) has been successfully targeted by both academia and the pharmaceutical industry for oncological and immunological applications. Typical proteasome inhibitors are based on a peptidic backbone endowed with an electrophilic C-terminus by which they react with the active proteolytic sites. Although the peptide moiety has attracted much attention in terms of subunit selectivity, the target specificity and biological stability of the compounds are largely determined by the reactive warheads. In this study, we have carried out a systematic investigation of described electrophiles by a combination of in vitro, in vivo, and structural methods in order to disclose the implications of altered functionality and chemical reactivity. Thereby, we were able to introduce and characterize the class of alpha-ketoamides as the most potent reversible inhibitors with possible applications for the therapy of solid tumors as well as autoimmune disorders.
Systematic Comparison of Peptidic Proteasome Inhibitors Highlights the alpha-Ketoamide Electrophile as an Auspicious Reversible Lead Motif.,Stein ML, Cui H, Beck P, Dubiella C, Voss C, Kruger A, Schmidt B, Groll M Angew Chem Int Ed Engl. 2014 Feb 3;53(6):1679-83. doi: 10.1002/anie.201308984., Epub 2014 Jan 8. PMID:24403024<ref>PMID:24403024</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nnw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Proteasome 3D structures|Proteasome 3D structures]]
*[[Proteasome 3D structures|Proteasome 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

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