| Literature DB >> 12651121 |
John F Vickrey1, Bradley C Logsdon, Gheorghe Proteasa, Sarah Palmer, Mark A Winters, Thomas C Merigan, Ladislau C Kovari.
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.Entities:
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Year: 2003 PMID: 12651121 DOI: 10.1016/s1046-5928(02)00650-2
Source DB: PubMed Journal: Protein Expr Purif ISSN: 1046-5928 Impact factor: 1.650