HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression,purification, and crystallization |
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Authors: | Vickrey John F Logsdon Bradley C Proteasa Gheorghe Palmer Sarah Winters Mark A Merigan Thomas C Kovari Ladislau C |
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Affiliation: | Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 E. Canfield Avenue, Detroit, MI 48201, USA. |
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Abstract: | High-resolution X-ray crystallographic structures of HIV-1 protease clinical variants complexed with licensed inhibitors are essential to understanding the fundamental cause of protease drug resistance. There is a need for structures of naturally evolved HIV-1 proteases from patients failing antiretroviral therapy. Here, we report the expression, purification, and crystallization of clinical isolates of HIV-1 protease that have been characterized to be more than 100 times less susceptible to US FDA approved protease inhibitors. |
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