COCRYSTAL STRUCTURE DATA OF HUMAN CYTOMEGALOVIRUS PROTEASE INHIBITOR COMPLEX

人巨细胞病毒蛋白水解酶是一种病毒丝氨酸水解酶 蛋白质组装体的蛋白质分解过程所必需的 巨细胞病毒衣壳成熟过程中的前体。阻滞剂 这种蛋白水解酶可能会被用作抗病毒药物 治疗移植患者和免疫低下患者的巨细胞病毒感染。 人巨细胞病毒蛋白水解酶催化结构域apo酶的X射线结构 在阿古伦得到解决，并发表在《细胞》，86：835-843(1996)。我们 正在采用基于结构的药物设计方法进行设计 抑制剂。使用强同步加速器X射线束，我们可以获得 缓蚀剂络合物的高分辨衍射数据。这个 结构信息将有助于使结构活动合理化 缓蚀剂之间的关系，将有助于设计和优化 针对疱疹病毒蛋白水解酶的新型抑制剂。

Human cytomegalovirus (HCMV) protease is a viral serine protease essential for proteolytic processing of the assembly of protein precursor during cytomegalovirus capsid maturation. Inhibitors to this protease may potentially be useful as antiviral agents for treating HCMV infection in transplant and immunocompromised patients. An X-ray structure of the HCMV protease catalytic domain apo enzyme was solved at Agouron and published in Cell, 86:835-843 (1996). We are taking the structure-based drug design approach to design inhibitors. Using the intense synchrotron X-ray beam we can obtain high resolution diffraction data of inhibitor complexes. The structure information will help to rationalize the structure-activity relationships of inhibitors and will aid the design and optimization of new inhibitors against herpesvirus proteases.