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Article

The N-terminal helix α(0) of hepatitis C virus NS3 protein dictates the subcellular localization and stability of NS3/NS4A complex.

Virology - 20 Jan 2012

He Ying, Weng Leiyun, Li Rui, Li Li, Toyoda Tetsuya, Zhong Jin

Abstract excerpt

The N-terminal amphipathic helix α(0) of hepatitis C virus (HCV) NS3 protein is an essential structural determinant for the protein membrane association. Here, we performed functional analysis to probe the role of this helix α(0) in the HCV life cycle. A point mutation M21P in this region that destroyed the helix formation disrupted the membrane association of NS3 protein and completely abolished HCV replication....

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Share to Cell Membrane
Share to Escherichia coli
Share to Gene Expression Regulation, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Stability

Share to Protein Structure, Secondary

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Source

Identifiers

PMID: 22088216
DOI: 10.1016/j.virol.2011.10.021

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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