Structural features of antiviral DNA cytidine deaminases

@inproceedings{Vasudevan2013StructuralFO,
  title={Structural features of antiviral DNA cytidine deaminases},
  author={Ananda Ayyappan Jaguva Vasudevan and Sander H. J. Smits and Astrid H{\"o}ppner and Dieter H{\"a}ussinger and Bernd W. Koenig and Carsten M{\"u}nk},
  booktitle={Biological chemistry},
  year={2013}
}
Abstract The APOBEC3 (A3) family of cytidine deaminases plays a vital role for innate defense against retroviruses. Lentiviruses such as HIV-1 evolved the Vif protein that triggers A3 protein degradation. There are seven A3 proteins, A3A-A3H, found in humans. All A3 proteins can deaminate cytidines to uridines in single-stranded DNA (ssDNA), generated during viral reverse transcription. A3 proteins have either one or two cytidine deaminase domains (CD). The CDs coordinate a zinc ion, and their… 

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