Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition.

@article{Bulliard2009FunctionalAA,
  title={Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition.},
  author={Yannick Bulliard and Priscilla Turelli and Ute F. R{\"o}hrig and Vincent Zoete and Bastien Mangeat and Olivier Michielin and Didier Trono},
  journal={Journal of virology},
  year={2009},
  volume={83 23},
  pages={12611-21}
}
Retroelements are important evolutionary forces but can be deleterious if left uncontrolled. Members of the human APOBEC3 family of cytidine deaminases can inhibit a wide range of endogenous, as well as exogenous, retroelements. These enzymes are structurally organized in one or two domains comprising a zinc-coordinating motif. APOBEC3G contains two such domains, only the C terminal of which is endowed with editing activity, while its N-terminal counterpart binds RNA, promotes homo… CONTINUE READING