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Literature summary for 3.4.21.91 extracted from

  • Yao, Y.; Huo, T.; Lin, Y.L.; Nie, S.; Wu, F.; Hua, Y.; Wu, J.; Kneubehl, A.R.; Vogt, M.B.; Rico-Hesse, R.; Song, Y.
    Discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease (2019), J. Am. Chem. Soc., 141, 6832-6836 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
drug development the enzyme is an important drug target Dengue virus
drug development the enzyme is an important drug target West Nile virus
drug development the enzyme is an important drug target Zika virus

Inhibitors

Inhibitors Comment Organism Structure
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
 Dengue virus
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
 West Nile virus
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
 Zika virus
additional information discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM). X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation Dengue virus
additional information discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM). X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation West Nile virus
additional information discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM) and in a mouse model of Zika virus infection. X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation Zika virus

Organism

Organism UniProt Comment Textmining
Dengue virus
-
 DENV
-
West Nile virus
-
 WNV
-
Zika virus
-
 ZIKV
-

Synonyms

Synonyms Comment Organism
flavivirus NS2B-NS3 protease
-
 Dengue virus
flavivirus NS2B-NS3 protease
-
 West Nile virus
flavivirus NS2B-NS3 protease
-
 Zika virus

General Information

General Information Comment Organism
evolution the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses Dengue virus
evolution the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses West Nile virus
evolution the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses Zika virus