A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease
Article Abstract:
A crystal structure analysis of the human cytomegalovirus (hCMV) at 2.0 Angstrom resolution reveals the hCMV protease to be made up of a polypeptide backbone fold having serine 132 and histidine 63 in close proximity at the active site. The structural features predict histidine 157 to be the third member of the triad, and the structure has a dimer of the protease with an extensive interface. The hCMV protease plays an important role in the production of mature infectious virions by proteolytic processing near the carboxy terminus of the viral assembly protein precursor.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus
Article Abstract:
The Hepatitis C virus (HCV)-encoded NS3 protease is essential for viral replication and was considered an attractive target for therapeutic intervention in HCV-infected patients. Results illustrate the potential of the viral-enzyme-targeted drug discovery approach for the development of new HCV therapeutics.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
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Modelling how ribavirin improves interferon response rates in hepatitis C virus infection
Article Abstract:
Nearly 200 million individuals worldwide are infected with hepatitis C virus (HCV). A model of HCV dynamics in which it is assumed that ribavirin decreases HCV infectivity in an infected indivudual in a dose-dependent manner is presented.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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