Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase

Article Abstract:

The non-structural protein NS5A is an active component of hepatitis C virus (HCV) replicase, as well as a pivotal regulator of replication and a modulator of cellular processes ranging from innate immunity to dysregulated cell growth. A report of the structure of NS5A domain I at 2.5-angstrom resolution, which contains a novel fold, a new zinc-coordination motif and a disulphide bond, is presented.

Proteins, Zinc compounds, Chemical properties

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Structure of the catalytic domain of the hepatitis C virus NS2-3 protease

Article Abstract:

The crystal structure of the catalytic domain of the hepatitis C virus NS2-3 protease at 2.3-Angstrom resolution is reported. The structure has revealed a dimeric cysteine protease with two composite active sites and these features have offered unexpected insights into polyprotein processing by hepatitis C virus and new opportunities for antiviral drug design.

New York, Analysis, Usage, Risk factors, Proteases, Crystals, Crystallization, Crystal growth, Structure, Ion exchange chromatography

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Unraveling Hepatitis C virus replication from genome to function

Article Abstract:

Researchers are studying each and every aspect of the life cycle of the Hepatitis C virus, right from the entry into the cytoplasm to its replication and the subsequent release from the cell. The genetic and biochemical approaches used in this area of research are likely to produce information that would help in the development of antiviral drugs.

Prevention, Genetic research, Cytoplasm

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