ArticleBiophysical journal2025
IP6, PF74 affect HIV-1 capsid stability through modulation of hexamer-hexamer tilt angle preference.
Article in Biophysical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Atomistic characterization of the maturation mechanisms in the HIV-1 capsid domain.Nature communications · 2026Article
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Abstract
The HIV-1 capsid is an irregularly shaped protein complex containing the viral genome and several proteins needed for integration into the host cell genome. Small molecules, such as the drug-like compound PF-3450074 (PF74) and the anionic sugar inositolhexakisphosphate (IP6), are known to impact capsid stability, although the mechanisms through which they do so remain unknown. In this study, we employed atomistic molecular dynamics simulations to study the impact of molecules bound to hexamers at the central pore (IP6) and the FG-binding site (PF74) on the interface between capsid oligomers. We found that the IP6 cofactor stabilizes a pair of neighboring hexamers in their flattest configurations, whereas PF74 introduces a strong preference for intermediate tilt angles. These results suggest that the tilt angle between neighboring hexamers is a primary mechanism for the modulation of capsid stability. In addition, hexamer-pentamer interfaces were highly stable, suggesting that pentamers are likely not the locus of disassembly.
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