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Crystal Structure of the Hepatitis C Virus NS3 Protease Domain Complexed with a Synthetic NS4A Cofactor Peptide
J.L Kim ,
K.A Morgenstern ,
C Lin ,
T Fox ,
M.D Dwyer ,
J.A Landro ,
S.P Chambers ,
W Markland ,
C.A Lepre ,
E.T O'Malley ,
S.L Harbeson ,
C.M Rice ,
M.A Murcko ,
P.R Caron ,
J.A Thomson
October 1996
October 1996
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Abstract
An estimated 1% of the global human population is infected by hepatitis C viruses
(HCVs), and there are no broadly effective treatments for the debilitating progression
of chronic hepatitis C. A serine protease located within the HCV NS3 protein processes
the viral polyprotein at four specific sites and is considered essential for replication.
Thus, it emerges as an attractive target for drug design. We report here the 2.5 angstrom
resolution X-ray crystal structure of the NS3 protease domain complexed with a synthetic
NS4A activator peptide. The protease has a chymotrypsin-like fold and features a tetrahedrally
coordinated metal ion distal to the active site. The NS4A peptide intercalates within
a beta sheet of the enzyme core.