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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Bibliografiske detaljer

Udgivet i:	J Virol
Principais autores:	Betakova, Tatiana, Moss, Bernard
Format:	Artigo
Sprog:	Inglês
Udgivet:	American Society for Microbiology (ASM) 2000
Fag:	Structure and Assembly
Online adgang:	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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