Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.

@article{Kim1998HepatitisCV,
  title={Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.},
  author={J L Kim and Kurt A Morgenstern and James P. Griffith and Mike Dwyer and James A. Thomson and Mark A. Murcko and C Lin and Paul R. Caron},
  journal={Structure},
  year={1998},
  volume={6 1},
  pages={89-100}
}
BACKGROUND Hepatitis C virus (HCV) represents a major health concern as it is responsible for a significant number of hepatitis cases worldwide. Much research has focused on the replicative enzymes of HCV as possible targets for more effective therapeutic agents. HCV NS3 helicase may provide one such suitable target. Helicases are enzymes which can unwind double-stranded regions of DNA or RNA in an ATP-dependent reaction. The structures of several helicases have been published but the… CONTINUE READING
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