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2V6N

Crystal structures of the SARS-coronavirus main proteinase inactivated by benzotriazole compounds

Summary for 2V6N
Entry DOI10.2210/pdb2v6n/pdb
DescriptorREPLICASE POLYPROTEIN 1AB, 4-(DIMETHYLAMINO)BENZOIC ACID, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (5 entities in total)
Functional Keywordsthiol protease, rna replication, main proteinase, ribosomal frameshift, sars, protease, hydrolase, polyprotein, viral protein
Biological sourceHUMAN SARS CORONAVIRUS (SARS-COV)
Total number of polymer chains1
Total formula weight34333.13
Authors
Verschueren, K.H.G.,Pumpor, K.,Anemueller, S.,Mesters, J.R.,Hilgenfeld, R. (deposition date: 2007-07-19, release date: 2008-07-01, Last modification date: 2024-10-16)
Primary citationVerschueren, K.H.G.,Pumpor, K.,Anemueller, S.,Chen, S.,Mesters, J.R.,Hilgenfeld, R.
A Structural View of the Inactivation of the Sars Coronavirus Main Proteinase by Benzotriazole Esters.
Chem.Biol., 15:597-, 2008
Cited by
PubMed Abstract: 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.
PubMed: 18559270
DOI: 10.1016/J.CHEMBIOL.2008.04.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.98 Å)
Structure validation

227561

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