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Literature summary for 3.4.21.98 extracted from

  • LaPlante, S.R.; Nar, H.; Lemke, C.T.; Jakalian, A.; Aubry, N.; Kawai, S.H.
    Ligand bioactive conformation plays a critical role in the design of drugs that target the hepatitis C virus NS3 protease (2014), J. Med. Chem., 57, 1777-1789.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with inhibitor N-(tert-butylcarbamoyl)-3-methyl-L-valyl-(4R)-N-[(1R,2S)-1-carboxy-2-ethenylcyclopropyl]-4-[(7-methoxy-2-phenylquinolin-4-yl)oxy]-L-prolinamide. The compound is bound to the active site of HCV protease through an anti-parallel beta-sheet between the inhibitor backbone and the E2-strand of the protease Hepacivirus C

Inhibitors

Inhibitors Comment Organism Structure
N-(tert-butylcarbamoyl)-3-methyl-L-valyl-(4R)-N-[(1R,2S)-1-carboxy-2-ethenylcyclopropyl]-4-[(7-methoxy-2-phenylquinolin-4-yl)oxy]-L-prolinamide inhibitor derived from peptide DDIVPC applying rigidification of the peptide scaffold to the bioactive conformation Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C Q0ZNA6
-
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00002
-
pH not specified in the publication, temperature not specified in the publication Hepacivirus C N-(tert-butylcarbamoyl)-3-methyl-L-valyl-(4R)-N-[(1R,2S)-1-carboxy-2-ethenylcyclopropyl]-4-[(7-methoxy-2-phenylquinolin-4-yl)oxy]-L-prolinamide