Myristylation of picornavirus capsid protein VP4 and its structural significance View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-06

AUTHORS

M Chow, J F Newman, D Filman, J M Hogle, D J Rowlands, F Brown

ABSTRACT

We have obtained evidence that poliovirus and other picornavirus particles are specifically modified by having myristic acid covalently bound to a capsid protein. The electron density map of poliovirus confirms the position of the myristate molecule and defines its location in the virus particle. Analogies with other myristylated proteins suggest that the myristate moiety in picornaviruses may be involved in capsid assembly or in the entry of virus into cells. More... »

PAGES

482-486

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/327482a0

DOI

http://dx.doi.org/10.1038/327482a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029482324

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3035380


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