Molecular model of the specificity pocket of the hepatitis C virus protease: implications for substrate recognition.

@article{Pizzi1994MolecularMO,
  title={Molecular model of the specificity pocket of the hepatitis C virus protease: implications for substrate recognition.},
  author={E Pizzi and Anna Tramontano and Licia Tomei and Nicola La Monica and Cristina Maria Failla and Mohita Sardana and T Wood and Raffaele De Francesco},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91},
  pages={888 - 892}
}
We have built a model of the specificity pocket of the protease of hepatitis C virus on the basis of the known structures of trypsin-like serine proteases and of the conservation pattern of the protease sequences among various hepatitis C strains. The model allowed us to predict that the substrate of this protease should have a cysteine residue in position P1. This hypothesis was subsequently proved by N-terminal sequencing of two products of the protease. The success of this "blind" test… 
Substrate Specificity of the Hepatitis C Virus Serine Protease NS3*
The substrate specificity of a purified protein encompassing the hepatitis C virus NS3 serine protease domain was investigated by introducing systematic modifications, including non-natural amino
Determinants of substrate specificity in the NS3 serine proteinase of the hepatitis C virus.
TLDR
Substitution of Phe-154 by alanine, by valine, and particularly by threonine generated enzymes with the following affinities for aliphatic P1 residues, suggesting an important role for this residue in substrate specificity.
The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism.
TLDR
The solution structure of the hepatitis C virus (BK strain) NS3 protein N-terminal domain (186 residues) has been solved by NMR spectroscopy and allows the formulation of a model in which, in addition to the NS4A cofactor, the substrate plays an important role in the activation of the catalytic mechanism.
The Hepatitis C Virus NS3 Proteinase: Structure and Function of a Zinc-Containing Serine Proteinase
TLDR
Starting from the observation that the NS3 proteinase undergoes product inhibition, very potent, active site-directed inhibitors have been generated using a combinatorial peptide chemistry approach.
The NS2 protein of hepatitis C virus is a transmembrane polypeptide
TLDR
It is demonstrated that theNS2 protein derived from processing at the NS2-3 site is a transmembrane polypeptide, with the C terminus translocated in the lumen of the ER and the N terminus located in the cytosol.
Hepatitis G Virus Encodes Protease Activities Which Can Effect Processing of the Virus Putative Nonstructural Proteins
ABSTRACT The genome of a recently identified virus, hepatitis G virus (HGV), shows considerable homology to hepatitis C virus (HCV). Two HGV proteases similar to nonstructural proteins NS2 and NS3 of
...
1
2
3
4
5
...