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Formation of transitory intrachain and interchain disulfide bonds accompanies the folding and oligomerization of simian virus 40 Vp1 in the cytoplasm
Pentamer formation by Vp1, the major capsid protein of simian virus 40, requires an interdigitation of structural elements from the Vp1 monomers [Liddington, R. C., Yan, Y., Moulai, J., Sahli, R., Benjamin, T. L. & Harrison, S. C. (1991) Nature (London) 354, 278–284]. Our analyses reveal that di...
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| Hoofdauteurs: | , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
The National Academy of Sciences
2002
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC122194/ https://ncbi.nlm.nih.gov/pubmed/11805304 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.032668699 |
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