Intermolecular interactions between the A and B subunits of heat-labile enterotoxin from Escherichia coli promote holotoxin assembly and stability in vivo.
Cholera toxin and the related heat-labile enterotoxin (LT) produced by Escherichia coli consist of a holotoxin of one A subunit and five B subunits (AB5). Here we investigate the domains of the A subunit (EtxA) of E. coli LT which influence the events of B-subunit (EtxB) oligomerization and the form...
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| Yayımlandı: | Proc Natl Acad Sci U S A |
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| Asıl Yazarlar: | , , , , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
National Academy of Sciences
1992
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC50714/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1465452/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.89.24.12140 |
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