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The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro
The N-terminal domain of the vaccinia virus protein E3L (Zα(E3L)) is essential for full viral pathogenicity in mice. It has sequence similarity to the high-affinity human Z-DNA-binding domains Zα(ADAR1) and Zα(DLM1). Here, we report the solution structure of Zα(E3L) and the chemical shift map of its...
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| Main Authors: | , , , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
National Academy of Sciences
2004
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC365686/ https://ncbi.nlm.nih.gov/pubmed/14981270 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0308612100 |
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