ArticleComputational and structural biotechnology journal2025
Flavivirus NS4B proteins do not form homodimers: discrepancies with an AlphaFold-based oligomeric model.
Article in Computational and structural biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Review
- Discovery of a potent anti-Zika virus benzamide series targeting the viral protein NS4B.PLoS pathogens · 2026Article
- Zika NS2B Protein: In Vitro Formation of Large Multimeric Networks.International journal of molecular sciences · 2026Article
- Discovery of a potent anti-Zika virus benzamide series targeting the viral protein NS4B.bioRxiv : the preprint server for biology · 2025Article
- AlphaFold in protein structure and function prediction.Computational and structural biotechnology journal · 2025Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In flaviviruses such as Dengue, Zika or West Nile virus (DENV, ZIKV or WNV), non-structural protein 4B (NS4B) participates in membrane remodeling during infection and is critical for virulence and host immunity. Despite the important roles and confirmed drug target status for NS4B, no detailed structure is available. Flavivirus NS4B proteins have five hydrophobic domains and have been proposed to form homodimers. Herein, we have used AlphaFold to explore its multimeric organization in a diverse set of five sequences of flaviviruses. AlphaFold correctly predicts the α-helical segments identified by solution NMR, but with a fold that differs from current models involving regular transmembrane helices. Oligomers of increasing size were evaluated using a combined AlphaFold score, with optimal value centered around decamers (
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