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Nat. Rev. Gastroenterol. Hepatol. doi:10.1038/nrgastro.2016.60 Figure 2 Location of resistance-associated amino acid substitutions in relation to drug binding Figure 2 | Location of resistance-associated amino acid substitutions in relation to drug binding. a | Crystal structure of NS3/4A protease in complex with the protease inhibitor asunaprevir (Protein Data Bank: 4WH6; Soumana, D. I. et al. ACS Chem. Biol. 9, 2485–2490 (2014)). The protease is shown in yellow and the inhibitor in blue. The Arg155Lys (R155K) substitution (red) is located in close proximity to the inhibitor. b | Crystal structure of NS5B (yellow) with primer (cyan), template (green), and the bound inhibitor (blue) sofosbuvir (Protein Data Bank: 4WTC; Appleby, T. C. et al. Science 347, 771–775 (2015)). Amino acids associated with decreased susceptibility to sofosbuvir are shown in red (Ser282) and magenta (Leu159). c | Structure of NS5A in the 'open' dimer conformation (left, Protein Data Bank: 1ZH1; Tellinghuisen, T. L. et al. Nature 435, 374–379 (2005)). Monomeric structures are shown in yellow and green. Changes at position Tyr93 (red) are associated with resistance to NS5A inhibitors. NS5A is also shown in a 'closed' conformation (right, Protein Data Bank: 3FQM; Love, R. A. et al. J. Virol. 83, 4395–4403 (2009)). Götte, M. & Feld, J. J. (2016) Direct-acting antiviral agents for hepatitis C: structural and mechanistic insights Nat. Rev. Gastroenterol. Hepatol. doi:10.1038/nrgastro.2016.60