A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility.

@article{Agopian2009ANG,
  title={A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility.},
  author={Audrey Agopian and Edwige Gros and Gudrun Aldrian-Herrada and Nathalie Bosquet and Pascal Clayette and Gilles Divita},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 1},
  pages={254-64}
}
The biologically active form of human immunodeficiency virus (HIV) type 1 reverse transcriptase (RT) is a heterodimer. The formation of RT is a two-step mechanism, including a rapid protein-protein interaction "the dimerization step," followed by conformational changes "the maturation step," yielding the biologically active form of the enzyme. We have previously proposed that the heterodimeric organization of RT constitutes an interesting target for the design of new inhibitors. Here, we… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

References

Publications referenced by this paper.

Reverse transcriptase and the generation of retroviral DNA

A. G. Telesnitsky, S.P
1997

Similar Papers

Loading similar papers…