Kinetic, Stability, and Structural Changes in High-resolution Crystal Structures of HIV-1 Protease with Drug-resistant Mutations L24I, I50V, and G73S

The crystal structures, dimer stabilities, and kinetics have been analyzed for wild-type human immunodeficiency virus type 1 (HIV-1) protease (PR) and resistant mutants PR(L24I), PR(I50V), and PR(G73S) to gain insight into the molecular basis of drug resistance. The mutations lie in different struct...

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Main Authors: Liu, Fengling, Boross, Peter I., Wang, Yuan-Fang, Tozser, Jozsef, Louis, John M., Harrison, Robert W., Weber, Irene T.
Formato: Artigo
Idioma:Inglês
Publicado: 2005
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Article
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC1403828/
https://ncbi.nlm.nih.gov/pubmed/16277992
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2005.09.095
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