Non-nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase. Crystal structures and mechanism of inhibition.

@article{Wang2003NonnucleosideAI,
  title={Non-nucleoside analogue inhibitors bind to an allosteric site on HCV NS5B polymerase. Crystal structures and mechanism of inhibition.},
  author={Meitian Wang and Kenneth K S Ng and Maia M. Cherney and Laval Chan and Constantin G. Yannopoulos and Jean H. B{\'e}dard and Nicolas Morin and Nghe Nguyen-Ba and Moulay Hicham Alaoui-Ismaili and Richard C. Bethell and Michael N. G. James},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 11},
  pages={9489-95}
}
X-ray crystal structures of two non-nucleoside analogue inhibitors bound to hepatitis C virus NS5B RNA-dependent RNA polymerase have been determined to 2.0 and 2.9 A resolution. These noncompetitive inhibitors bind to the same site on the protein, approximately 35 A from the active site. The common features of binding include a large hydrophobic region and two hydrogen bonds between both oxygen atoms of a carboxylate group on the inhibitor and two main chain amide nitrogen atoms of Ser(476) and… CONTINUE READING

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