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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| Gepubliceerd in: | J Virol |
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| Hoofdauteurs: | , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
American Society for Microbiology (ASM)
2000
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| Onderwerpen: | |
| Online toegang: | 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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