EC Number   |
Inhibitors |
Structure  |
|---|
   3.4.21.98 | more |
alpha-ketoacids incorporating difluoroaminobutyric acid in the p1 position are potent slow binding inhibitors |
 |
| 3.4.21.98 | more |
many NS3 protease inhibitors have taken advantage of an unusual product inhibition by N-terminal products of cleavage at the polyprotein processing sites |
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| 3.4.21.98 | more |
solid-phase synthesis of peptidomimetic inhibitors |
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| 3.4.21.98 | more |
the effect of prime-site occupancy on the enzyme structure |
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| 3.4.21.98 | more |
inhibitors with electrophilic C-terminal residues are generally non-selective while compounds with non-electrophilic C-terminal residues are more selective. Compounds with P1 aminobutyric acid residues are non-selective, while 1-aminocyclopropanecarboxylic acid and norvaline-based inhibitors are generally selective. Most potent and selective inhibitors contain a non-electrophilic phenyl acyl sulfonamide C-terminal residue |
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| 3.4.21.98 | more |
the P1 and P2 positions are most important for inhibitor binding, whilst the P3 and P4 positions have much less effect |
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| 3.4.21.98 | more |
human leukocyte antigen A2restricted epitope in which substitutions at 5 of 9 residues destroy the protease |
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| 3.4.21.98 | more |
EGTA and zinc metalloprotease inhibitors bestatin, phosphoramidon and thiorphan have no effect on NS2/3 auto-cleavage and NS3 protease activity. No inhibitory effect of the NS4A peptide on NS2/3 auto-cleavage, additionally the NS4A peptide does not significantly affect the sensitivity of NS2/3 autocleavage to zinc chelation, but has a marked effect on NS3 protease activity, rendering this activity approximately 3fold more resistant to zinc chelation |
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| 3.4.21.98 | more |
methylated 3,3'-digalloylproprodelphinidin B2, hexanoylated (-)-epigallocatechin-3-O-gallate, (-)-epigallocatechin, (-)-epicatechin, gallic acid, luetolin, tyrosol and salidroside show no activity up to 100 micromol |
|
| 3.4.21.98 | more |
two galloyl residues at 3 and 4 positions of the glucopyranose ring of the plant inhibitors interact with SER139, GLY137, ALA157, and ASP81 by hydrogen bond interaction and with ALA156 and HIE57 by hydrophobic interaction and are essential for the activities of the inhibitors |
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