The crystal structure of one of the hepatitis C viral proteins could offer new opportunities for antiviral drug design, report Charles Rice and colleagues in a paper published online by Nature. The disease affects an estimated 170 million people worldwide, often leading to cirrhosis and liver cancer.
The viral genome encodes a single polyprotein, which cleaves into proteins including the NS2-3 protease. The crystal structure of the protease catalytic domain reveals a novel structure: it is actually a dimer (resembling a 'butterfly') composed of two identical proteins that each contributes amino acids to two equivalent active sites. The concentration and dimerization of NS2-3 may be a limiting factor in the viral life cycle because the protease is essential for viral replication. Details of the structure may help in the search for small-molecule inhibitors directed against the active site.
Charles Rice (The Rockefeller University, New York, NY, USA)
(C) Nature press release.
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