Structures of Darunavir-Resistant HIV-1 Protease Mutant Reveal Atypical Binding of Darunavir to Wide Open Flaps

[Image: see text] The molecular basis for high resistance to clinical inhibitors of HIV-1 protease (PR) was examined for the variant designated PR(P51) that was selected for resistance to darunavir (DRV). High resolution crystal structures of PR(P51) with the active site D25N mutation revealed a lig...

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Detalles Bibliográficos
Autores principales: Zhang, Ying, Chang, Yu-Chung E., Louis, John M., Wang, Yuan-Fang, Harrison, Robert W., Weber, Irene T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4076034/
https://www.ncbi.nlm.nih.gov/pubmed/24738918
http://dx.doi.org/10.1021/cb4008875

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4076034/
https://www.ncbi.nlm.nih.gov/pubmed/24738918
http://dx.doi.org/10.1021/cb4008875

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