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Active Sites Of A Hepatitis C Virus Enzyme Revealed

 
  August, 2 2006 8:59
your information resource in human molecular genetics
 
     
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.

CONTACT

Charles Rice (The Rockefeller University, New York, NY, USA)
E-mail: ricec@rockefeller.edu

(C) Nature press release.


Message posted by: Trevor M. D'Souza

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