Disulfide Bonds and Membrane Topology of the Vaccinia Virus A17L Envelope Protein

The envelope protein encoded by the vaccinia virus A17L open reading frame is essential for virion assembly. Our mutagenesis studies indicated that cysteines 101 and 121 form an intramolecular disulfide bond and that cysteine 178 forms an intermolecular disulfide linking two A17L molecules. This arr...

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Опубликовано в::	J Virol
Главные авторы:	Betakova, Tatiana, Moss, Bernard
Формат:	Artigo
Язык:	Inglês
Опубликовано:	American Society for Microbiology (ASM) 2000
Предметы:	Structure and Assembly
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC111727/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10666276/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.74.5.2438-2442.2000
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