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...

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Detalles Bibliográficos
Autores principales: Ung, Peter M.-U., Dunbar, James B., Gestwicki, Jason E., Carlson, Heather A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4136727/
https://www.ncbi.nlm.nih.gov/pubmed/25062388
http://dx.doi.org/10.1021/jm5008352

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4136727/
https://www.ncbi.nlm.nih.gov/pubmed/25062388
http://dx.doi.org/10.1021/jm5008352

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