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An Allosteric Modulator of HIV-1 Protease Shows Equipotent Inhibition of Wild-Type and Drug-Resistant Proteases
[Image: see text] 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 HIV-1p, called the Eye sit...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Chemical
Society
2014
|
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4136727/ https://ncbi.nlm.nih.gov/pubmed/25062388 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jm5008352 |
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