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Literature summary for 3.4.21.98 extracted from

  • Di Marco, S.; Rizzi, M.; Volpari, C.; Walsh, M.A.; Narjes, F.; Colarusso, S.; De Francesco, R.; Matassa, V.G.; Sollazzo, M.
    Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes (2000), J. Biol. Chem., 275, 7152-7157.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method, crystal structure of the protease domain with a chymotrypsin-like fold, complexed with NS4 cofactor and with two potent, reversible covalent inhibitors spanning the P1-P4 residues,tert-butyloxacrybonyl-L-Glu-L-Leu-L-(difluoro)aminobutyric acid and benzyloxycarbonyl-L-Ile-L-Leu-L-(difluoro)aminobutyric acid Hepacivirus C

Inhibitors

Inhibitors Comment Organism Structure
benzyloxycarbonyl-L-Ile-L-Leu-L-(difluoro)aminobutyric acid
-
Hepacivirus C
tert-butyloxacrybonyl-L-Glu-L-Leu-L-(difluoro)aminobutyric acid
-
Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
-
-

Synonyms

Synonyms Comment Organism
NS3/4A protease
-
Hepacivirus C