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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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Bibliografiske detaljer
Main Authors: Moscufo, N, Chow, M
Format: Artigo
Sprog:Inglês
Udgivet: 1992
Fag:
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC240287/
https://ncbi.nlm.nih.gov/pubmed/1331497
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