Structural integrity of the ribonuclease H domain in HIV-1 reverse transcriptase.

@article{Slack2015StructuralIO,
  title={Structural integrity of the ribonuclease H domain in HIV-1 reverse transcriptase.},
  author={Ryan L Slack and Justin Spiriti and Jinwoo Ahn and Michael A. Parniak and Daniel M. Zuckerman and Rieko Ishima},
  journal={Proteins},
  year={2015},
  volume={83 8},
  pages={1526-38}
}
The mature form of reverse transcriptase (RT) is a heterodimer comprising the intact 66-kDa subunit (p66) and a smaller 51-kDa subunit (p51) that is generated by removal of most of the RNase H (RNH) domain from a p66 subunit by proteolytic cleavage between residues 440 and 441. Viral infectivity is eliminated by mutations such as F440A and E438N in the proteolytic cleavage sequence, while normal processing and virus infectivity are restored by a compensatory mutation, T477A, that is located… CONTINUE READING
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