Mechanism of drug resistance revealed by the crystal structure of the unliganded HIV-1 protease with F53L mutation.

@article{Liu2006MechanismOD,
  title={Mechanism of drug resistance revealed by the crystal structure of the unliganded HIV-1 protease with F53L mutation.},
  author={Fengling Liu and Andrey Y Kovalevsky and John M. Louis and Peter I Boross and Yuan-Fang Wang and Robert W. Harrison and Irene T. Weber},
  journal={Journal of molecular biology},
  year={2006},
  volume={358 5},
  pages={1191-9}
}
Mutations in HIV-1 protease (PR) that produce resistance to antiviral PR inhibitors are a major problem in AIDS therapy. The mutation F53L arising from antiretroviral therapy was introduced into the flexible flap region of the wild-type PR to study its effect and potential role in developing drug resistance. Compared to wild-type PR, PR(F53L) showed lower (15%) catalytic efficiency, 20-fold weaker inhibition by the clinical drug indinavir, and reduced dimer stability, while the inhibition… CONTINUE READING

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