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==CRYSTAL STRUCTURES OF THE SARS-CORONAVIRUS MAIN PROTEINASE INACTIVATED BY BENZOTRIAZOLE COMPOUNDS== | |||
[[Image: | <StructureSection load='2v6n' size='340' side='right' caption='[[2v6n]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2v6n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V6N FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XP1:4-(DIMETHYLAMINO)BENZOIC+ACID'>XP1</scene><br> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v6n RCSB], [http://www.ebi.ac.uk/pdbsum/2v6n PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v6/2v6n_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The main proteinase (M(pro)) of the severe acute respiratory syndrome (SARS) coronavirus is a principal target for the design of anticoronaviral compounds. Benzotriazole esters have been reported as potent nonpeptidic inhibitors of the enzyme, but their exact mechanism of action remains unclear. Here we present crystal structures of SARS-CoV M(pro), the active-site cysteine of which has been acylated by benzotriazole esters that act as suicide inhibitors. In one of the structures, the thioester product has been hydrolyzed and benzoic acid is observed to bind to the hydrophobic S2 pocket. This structure also features the enzyme with a shortened N-terminal segment ("amputated N finger"). The results further the understanding of the important role of the N finger for catalysis as well as the design of benzotriazole inhibitors with improved specificity. | |||
A structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters.,Verschueren KH, Pumpor K, Anemuller S, Chen S, Mesters JR, Hilgenfeld R Chem Biol. 2008 Jun;15(6):597-606. PMID:18559270<ref>PMID:18559270</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Sars coronavirus]] | |||
== | |||
< | |||
[[Category: | |||
[[Category: Anemueller, S.]] | [[Category: Anemueller, S.]] | ||
[[Category: Hilgenfeld, R.]] | [[Category: Hilgenfeld, R.]] | ||
| Line 39: | Line 43: | ||
[[Category: Thiol protease]] | [[Category: Thiol protease]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
Revision as of 13:26, 28 May 2014
CRYSTAL STRUCTURES OF THE SARS-CORONAVIRUS MAIN PROTEINASE INACTIVATED BY BENZOTRIAZOLE COMPOUNDSCRYSTAL STRUCTURES OF THE SARS-CORONAVIRUS MAIN PROTEINASE INACTIVATED BY BENZOTRIAZOLE COMPOUNDS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe main proteinase (M(pro)) of the severe acute respiratory syndrome (SARS) coronavirus is a principal target for the design of anticoronaviral compounds. Benzotriazole esters have been reported as potent nonpeptidic inhibitors of the enzyme, but their exact mechanism of action remains unclear. Here we present crystal structures of SARS-CoV M(pro), the active-site cysteine of which has been acylated by benzotriazole esters that act as suicide inhibitors. In one of the structures, the thioester product has been hydrolyzed and benzoic acid is observed to bind to the hydrophobic S2 pocket. This structure also features the enzyme with a shortened N-terminal segment ("amputated N finger"). The results further the understanding of the important role of the N finger for catalysis as well as the design of benzotriazole inhibitors with improved specificity. A structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters.,Verschueren KH, Pumpor K, Anemuller S, Chen S, Mesters JR, Hilgenfeld R Chem Biol. 2008 Jun;15(6):597-606. PMID:18559270[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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