The Nonstructural Protein 3 Protease/Helicase Requires an Intact Protease Domain to Unwind Duplex RNA Efficiently

View Full Paper

Ask AI

Bookmark

Population

Hepatitis C virus nonstructural 3 (NS3) protein

Comparison

Truncated versions of NS3 protein vs Full-length NS3 protein

Design

Preclinical

Authors

Discussion

Hypothesis-generating for NS3 domain coordination in HCV; extends biochemical models of helicase regulation.

Population

Hepatitis C virus nonstructural 3 (NS3) protein

Intervention

Truncated versions of NS3 protein (protease domain deleted or replaced by His tag or GST tag)

Comparator

Full-length NS3 protein

Outcome

RNA helicase activity (unwinding speed, ATP hydrolysis, and binding properties)

The protease domain of the hepatitis C virus NS3 protein is required for efficient RNA unwinding and ATP usage by the helicase domain.

Frick et al. (2004) studied this question.

View Full Paper

Ask AI

Bookmark