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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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Detaylı Bibliyografya
Asıl Yazarlar: Kahmann, Jan D., Wecking, Diana A., Putter, Vera, Lowenhaupt, Ky, Kim, Yang-Gyun, Schmieder, Peter, Oschkinat, Hartmut, Rich, Alexander, Schade, Markus
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: National Academy of Sciences 2004
Konular:
Online Erişim: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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