Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase.
Yao, N., Reichert, P., Taremi, S.S., Prosise, W.W., Weber, P.C.(1999) Structure 7: 1353-1363
- PubMed: 10574797 
- DOI: https://doi.org/10.1016/s0969-2126(00)80025-8
- Primary Citation of Related Structures:  
1CU1 - PubMed Abstract: 
Hepatitis C virus (HCV) currently infects approximately 3% of the world's population. HCV RNA is translated into a polyprotein that during maturation is cleaved into functional components. One component, nonstructural protein 3 (NS3), is a 631-residue bifunctional enzyme with protease and helicase activities. The NS3 serine protease processes the HCV polyprotein by both cis and trans mechanisms. The structural aspects of cis processing, the autoproteolysis step whereby the protease releases itself from the polyprotein, have not been characterized. The structural basis for inclusion of protease and helicase activities in a single polypeptide is also unknown.
Organizational Affiliation: 
Structural Chemistry Department, Schering-Plough Research Institute, Kenilworth, NJ 07033-0539, USA.