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Literature summary for 3.4.21.98 extracted from

  • Abian, O.; Vega, S.; Sancho, J.; Velazquez-Campoy, A.
    Allosteric inhibitors of the NS3 protease from the hepatitis C virus (2013), PLoS ONE, 8, e69773.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.98

Protein Variants

Protein Variants Comment Organism
S139A inactive Hepacivirus C

Inhibitors

Inhibitors Comment Organism Structure
1,2,3,4-tetrahydroacridin-9-amine inhibitor binding to Zn2+-free enzyme, dissociation constant 0.0017 mM, EC50 value 0.060 mM Hepacivirus C
methyl [5-(thiophen-2-ylcarbonyl)-1H-benzimidazol-2-yl]carbamate inhibitor binding to Zn2+-free enzyme, dissociation constant 0.0019 mM, EC50 value 0.00003 mM Hepacivirus C
additional information in the absence of Zn+2, the NS3 protease adopts a partially-folded inactive conformation. Identification of ligands binding to the Zn+2-free NS3 protease, that trap the inactive protein, and block the viral life cycle. Ligands show a new inhibition mechanism simultaneously blocking substrate and cofactor interactions in a non-competitive fashion, appropriate for combination therapy, low impact of known resistance-associated mutations and inhibition of NS4A binding, thus blocking its several effects on NS3 protease Hepacivirus C

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ in the absence of Zn+2, the NS3 protease adopts a partially-folded inactive conformation Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
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