The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding Site

@article{Love1996TheCS,
  title={The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding Site},
  author={Robert A. Love and Hans E. Parge and John A Wickersham and Zdenek Hostomsky and Noriyuki Habuka and Ellen W Moomaw and Tsuyoshi Adachi and Zuzana Hostomska},
  journal={Cell},
  year={1996},
  volume={87},
  pages={331-342}
}
During replication of hepatitis C virus (HCV), the final steps of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of nonstructural protein 3. The structure of NS3 proteinase from HCV BK strain was determined by X-ray crystallography at 2.4 angstrom resolution. NS3P folds as a trypsin-like proteinase with two beta barrels and a catalytic triad of His-57, Asp-81, Ser-139. The structure has a substrate-binding site consistent with the cleavage… CONTINUE READING
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