Unique composite active site of the hepatitis C virus NS2-3 protease: a new opportunity for antiviral drug design.
Suo
Zucai
Z
Department of Biochemistry, The Ohio State University, 484 W. 12th Ave., Biological Sciences Building, Columbus, OH 43210, USA. suo.3@osu.edu
Abdullah
Mohd Amir F
MA
D019943:Amino Acid Substitution; D000998:Antiviral Agents / Q000737:chemistry / Q000494:pharmacology*; D001665:Binding Sites; D020134:Catalytic Domain; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015195:Drug Design; D016174:Hepacivirus / Q000187:drug effects* / Q000201:enzymology; D008958:Models, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000998:Antiviral Agents; D003546:Cysteine Endopeptidases; C107824:NS2-3 protease