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Article

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.

The Journal of biological chemistry - 10 Jun 2011

Verdegem Dries, Badillo Aurélie, Wieruszeski Jean-Michel, Landrieu Isabelle, Leroy Arnaud, Bartenschlager Ralf, Penin François, Lippens Guy, Hanoulle Xavier

Abstract excerpt

Nonstructural protein 5A (NS5A) is essential for hepatitis C virus (HCV) replication and constitutes an attractive target for antiviral drug development. Although structural data for its in-plane membrane anchor and domain D1 are available, the structure of domains 2 (D2) and 3 (D3) remain poorly defined. We report here a comparative molecular characterization of the NS5A-D3 domains of the HCV JFH-1 (genotype 2a)...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 21489988
DOI: 10.1074/jbc.M110.182436
PMCID: PMC3121464

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