Structural highlights
Function
[A7J8L3_CVHSA] Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).[SAAS:SAAS008740_004_014545] Nsp9 is a ssRNA-binding protein (By similarity).[SAAS:SAAS008740_004_001449]
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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Verschueren KH, Pumpor K, Anemuller S, Chen S, Mesters JR, Hilgenfeld R. A structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters. Chem Biol. 2008 Jun;15(6):597-606. PMID:18559270 doi:10.1016/j.chembiol.2008.04.011
