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An allosteric modulator of HIV-1 protease shows equipotent inhibition of wild-type and drug-resistant proteases

  • Author(s): Gestwicki, Jason
  • Ung, PMU
  • Dunbar, JB
  • Gestwicki, JE
  • Carlson, HA
  • et al.

Published Web Location

http://europepmc.org/articles/PMC4136727?pdf=render
No data is associated with this publication.
Abstract

NMR and MD simulations have demonstrated that the flaps of HIV-1 protease (HIV-1p) adopt a range of conformations that are coupled with its enzymatic activity. Previously, a model was created for an allosteric site located between the flap and the core of

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