Myristate-protein interactions in poliovirus: interactions of VP4 threonine 28 contribute to the structural conformation of assembly intermediates and the stability of assembled virions.
The VP4 capsid protein of poliovirus is N-terminally modified with myristic acid. Within the poliovirus structure, a hydrogen bond is observed between the myristate carbonyl and the hydroxyl side chain of threonine 28 of VP4. This interaction is between two fivefold symmetry-related copies of VP4 an...
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| Veröffentlicht in: | J Virol |
|---|---|
| Hauptverfasser: | , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
American Society for Microbiology (ASM)
1992
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| Schlagworte: | |
| Online-Zugang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC240287/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1331497/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.66.12.6849-6857.1992 |
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