| STRUCTURE |
Light shed on hepatitis C replication © NATURE 2005 Scientists have produced the first molecular-level glimpse at a protein that plays a crucial role in replication of the hepatitis C virus (HCV) (Nature 2005, 435, 374). Nearly 3% of the world's population is infected with HCV, which can lead to cirrhosis and liver cancer. Charles M. Rice, Timothy L. Tellinghuisen, and Joseph Marcotrigiano of Rockefeller University hope that their crystal structure of a portion of NS5A--an active component of the multisubunit machine that HCV uses to replicate its RNA genome--will lead not only to a better understanding of how HCV replicates itself but also to the development of replication inhibitors to combat HCV infections. Their 2.5-Å-resolution structure (shown) reveals that domain I of NS5A has a novel fold, an unexpected disulfide bond, and an unusual four-cysteine zinc-coordination motif. The researchers suggest that the protein's zinc (yellow sphere) plays a structural, not catalytic, role. In the crystal, two molecules of domain I are packed against each other to create a deep groove that might bind RNA to be replicated, they propose. |
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