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Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces
APOBEC3G is a DNA cytidine deaminase that has anti-viral activity against HIV-1 and other pathogenic viruses. In this study the crystal structure of the catalytically active C-terminal domain was determined to 2.25 Å. This structure corroborates features previously observed in NMR studies, a bulge i...
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| Hlavní autoři: | , , , , , , , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2010
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2913127/ https://ncbi.nlm.nih.gov/pubmed/20152150 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2009.10.016 |
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