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Literature summary for 3.4.21.98 extracted from

  • Soderholm, J.; Sallberg, M.
    A complete mutational fitness map of the hepatitis C virus nonstructural 3 protease: Relation to recognition by cytotoxic T lymphocytes (2006), J. Infect. Dis., 194, 1724-1728.
    View publication on PubMed

Application

Application Comment Organism
drug development design of epitope-based vaccines, where epitopes preferably should be those in which the virus is unable to mutate due to viral fitness Hepacivirus C

Protein Variants

Protein Variants Comment Organism
additional information sequentially mutated 180 protease-domain residues to Ala or Gly in a functional full-length NS3/4A gene. Most (87%) protease residues can be replaced and protease activity is retained, suggesting that the protease has an unexpectedly high plasticity Hepacivirus C

Inhibitors

Inhibitors Comment Organism Structure
additional information human leukocyte antigen A2–restricted epitope in which substitutions at 5 of 9 residues destroy the protease Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
nonstructural 3 protease
-
Hepacivirus C
NS3 protease
-
Hepacivirus C
NS3/4A protease
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Hepacivirus C