6n80

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'''Unreleased structure'''
 
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The entry 6n80 is ON HOLD until Paper Publication
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==S. aureus ClpP bound to anti-4a==
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<StructureSection load='6n80' size='340' side='right'caption='[[6n80]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6n80]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N80 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JT7:N-[(1R)-1-borono-3-methylbutyl]-N~2~-(2-chloro-4-methoxybenzene-1-carbonyl)-L-leucinamide'>JT7</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr>
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<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=6n80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n80 OCA], [http://pdbe.org/6n80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n80 RCSB], [http://www.ebi.ac.uk/pdbsum/6n80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n80 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CLPP_STAA8 CLPP_STAA8]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Boronic acids have attracted the attention of synthetic and medicinal chemists due to boron's ability to modulate enzyme function. Recently, we demonstrated that boron-containing amphoteric building blocks facilitate the discovery of bioactive aminoboronic acids. Herein, we have augmented this capability with a de novo library design and virtural screening platform modified for covalent ligands. This technique has allowed us to rapidly design and identify a series of alpha-aminoboronic acids as the first inhibitors of human ClpXP, which is responsible for the degradation of misfolded proteins.
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Authors: Lee, R.E., Griffith, E.C.
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De novo design of boron-based peptidomimetics as potent inhibitors of human ClpP in the presence of human ClpX.,Tan J, Grouleff JG, Jitkova Y, Diaz DB, Griffith E, Shao W, Bogdanchikova AF, Poda G, Schimmer AD, Lee RE, Yudin AK J Med Chem. 2019 Jun 12. doi: 10.1021/acs.jmedchem.9b00878. PMID:31187989<ref>PMID:31187989</ref>
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Description: S. aureus ClpP bound to anti-4a
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Griffith, E.C]]
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<div class="pdbe-citations 6n80" style="background-color:#fffaf0;"></div>
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[[Category: Lee, R.E]]
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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: Endopeptidase Clp]]
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[[Category: Large Structures]]
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[[Category: Griffith, E C]]
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[[Category: Lee, R E]]
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[[Category: Clpp]]
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[[Category: Hydrolase]]

Revision as of 06:56, 26 June 2019

S. aureus ClpP bound to anti-4a

PDB ID 6n80

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