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 Locationhttp://europepmc.org/articles/PMC4136727?pdf=render
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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