Model Structure of Human APOBEC3G

  title={Model Structure of Human APOBEC3G},
  author={Kunlin Zhang and B. Mangeat and M. Ortiz and V. Zoete and D. Trono and A. Telenti and O. Michielin},
  journal={PLoS ONE},
  • Kunlin Zhang, B. Mangeat, +4 authors O. Michielin
  • Published 2007
  • Biology, Medicine
  • PLoS ONE
  • Background APOBEC3G (apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G) has antiretroviral activity associated with the hypermutation of viral DNA through cytosine deamination. APOBEC3G has two cytosine deaminase (CDA) domains; the catalytically inactive amino-terminal domain of APOBEC3G (N-CDA) carries the Vif interaction domain. There is no 3-D structure of APOBEC3G solved by X-ray or nuclear magnetic resonance. Methodology/Principal Findings We predicted the structure of… CONTINUE READING

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