HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression, purification, and crystallization
HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression, purification, and crystallization
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DOI：
10.1016/s1046-5928(02)00650-2
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发表时间：
2003-03-01
影响因子：
1.6
通讯作者：
Kovari, LC
中科院分区：
文献类型：
--
作者：
Vickrey, JF;Logsdon, BC;Kovari, LC
HIV-1蛋白酶临床变异与许可抑制剂的高分辨率x射线晶体结构对于了解蛋白酶耐药的根本原因至关重要。需要从抗逆转录病毒治疗失败的患者那里自然进化的HIV-1蛋白酶结构。在这里，我们报道了HIV-1蛋白酶临床分离株的表达、纯化和结晶，其特征是对美国FDA批准的蛋白酶抑制剂的敏感性降低了100倍以上。(C) 2002 Elsevier Science （USA）。版权所有。
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. (C) 2002 Elsevier Science (USA). All rights reserved.