来自100倍耐药临床分离株的HIV-1蛋白酶变体：表达、纯化及结晶
HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression, purification, and crystallization.
作者信息
Vickrey John F, Logsdon Bradley C, Proteasa Gheorghe, Palmer Sarah, Winters Mark A, Merigan Thomas C, Kovari Ladislau C
机构信息
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 E. Canfield Avenue, Detroit, MI 48201, USA.
出版信息
Protein Expr Purif. 2003 Mar;28(1):165-72. doi: 10.1016/s1046-5928(02)00650-2.
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.
与已获许可的抑制剂复合的HIV-1蛋白酶临床变体的高分辨率X射线晶体结构对于理解蛋白酶耐药性的根本原因至关重要。对于接受抗逆转录病毒治疗失败的患者体内自然进化的HIV-1蛋白酶的结构存在需求。在此，我们报告了已被鉴定为对美国食品药品监督管理局批准的蛋白酶抑制剂敏感性降低100倍以上的HIV-1蛋白酶临床分离株的表达、纯化和结晶情况。
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