The Hepatitis C Virus Life Cycle as a Target for New Antiviral Therapies  Jean–Michel Pawlotsky, Stéphane Chevaliez, John G. McHutchison  Gastroenterology  Volume 132, Issue 5, Pages 1979-1998 (May 2007) DOI: 10.1053/j.gastro.2007.03.116 Copyright © 2007 AGA Institute Terms and Conditions

Figure 1 Current status of HCV life cycle inhibitors in preclinical or clinical development. Gastroenterology 2007 132, 1979-1998DOI: (10.1053/j.gastro.2007.03.116) Copyright © 2007 AGA Institute Terms and Conditions

Figure 2 Schematic representation of the HCV life cycle. Every step of the life cycle offers a variety of potential targets for novel drug classes. Gastroenterology 2007 132, 1979-1998DOI: (10.1053/j.gastro.2007.03.116) Copyright © 2007 AGA Institute Terms and Conditions

Figure 3 Ribbon diagram of the crystal structure of the full-length NS3 protein showing the NS3 serine proteinase domain (cyan) associated with the central NS4A protease activation domain (yellow). Side-chain atoms of the catalytic-triad amino acids (His 57, Asp 81, and Ser 139) are represented as magenta spheres of the corresponding van der Waals radius. NS3 helicase domains I, II, and III are colored in silver, red, and blue, respectively. PDB accession codes: 1CU1. Potential target sites for specific antiviral molecules are shown. Gastroenterology 2007 132, 1979-1998DOI: (10.1053/j.gastro.2007.03.116) Copyright © 2007 AGA Institute Terms and Conditions

Figure 4 Ribbon diagram of the HCV RNA-dependent RNA polymerase. The fingers, palm, and thumb subdomains are colored in blue, red, and green, respectively. The catalytic site lies within the center of the ectodomain. The β-loop is colored in orange. PDB accession code: 1GX6. Five target sites for antiviral molecules have been identified so far, including the enzyme catalytic site and nonnucleoside inhibitor (NNI) allosteric sites A to D. Gastroenterology 2007 132, 1979-1998DOI: (10.1053/j.gastro.2007.03.116) Copyright © 2007 AGA Institute Terms and Conditions