6l5t

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'''Unreleased structure'''
 
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The entry 6l5t is ON HOLD until Oct 24 2021
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==The crystal structure of SADS-CoV Papain Like protease==
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<StructureSection load='6l5t' size='340' side='right'caption='[[6l5t]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6l5t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L5T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L5T FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l5t OCA], [http://pdbe.org/6l5t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l5t RCSB], [http://www.ebi.ac.uk/pdbsum/6l5t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l5t ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Swine acute diarrhea syndrome coronavirus (SADS-CoV) is a novel coronavirus that is involved in severe diarrhea disease in piglets, causing considerable agricultural and economic loss in China. The emergence of this new coronavirus increases the importance of understanding SADS-CoV as well as antivirals. Coronaviral proteases, including main proteases and papain-like proteases (PLP), are attractive antiviral targets because of their essential roles in polyprotein processing and thus viral maturation. Here, we describe the biochemical and structural identification of recombinant SADS papain-like protease 2 (PLP2) domain of nsp3. The SADS-CoV PLP2 was shown to cleave nsp1 proteins and also peptides mimicking the nsp2|nsp3 cleavage site and also had deubiquitinating and deISGynating activity by in vitro assays. The crystal structure adopts an architecture resembling that of PLPs from other coronaviruses. We characterize both conserved and unique structural features likely directing the interaction of PLP2 with the substrates, including the tentative mapping of active site and other essential residues. These results provide a foundation for understanding the molecular basis of coronaviral PLPs' catalytic mechanism and for the screening and design of therapeutics to combat infection by SADS coronavirus.
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Authors:
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Structural and biochemical characterization of SADS-CoV papain-like protease 2.,Wang L, Hu W, Fan C Protein Sci. 2020 Mar 26. doi: 10.1002/pro.3857. PMID:32216114<ref>PMID:32216114</ref>
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Description:
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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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<div class="pdbe-citations 6l5t" style="background-color:#fffaf0;"></div>
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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: Fan, C P]]
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[[Category: Hydrolase]]
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[[Category: Protease]]

Revision as of 06:48, 8 April 2020

The crystal structure of SADS-CoV Papain Like protease

PDB ID 6l5t

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