Russo Andrew T, Watowich Stanley J
Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):514-7. doi: 10.1107/S1744309106014667. Epub 2006 May 5.
The C-terminal region of Venezuelan equine encephalitis virus (VEEV) nsP2 is responsible for proteolytic processing of the VEEV polyprotein replication complex. This action regulates the activity of the replication complex and is essential for viral replication, thus making nsP2 a very attractive target for development of VEEV therapeutics. The 338-amino-acid C-terminal region of VEEV nsP2 has been overexpressed in Escherichia coli, purified and crystallized. Crystals diffract to beyond 2.5 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1). Isomorphous heavy-atom derivatives suitable for phase analysis have been obtained and work on building a complete structural model is under way.
委内瑞拉马脑炎病毒（VEEV）非结构蛋白2（nsP2）的C末端区域负责VEEV多蛋白复制复合体的蛋白水解加工。这一作用调节复制复合体的活性，对病毒复制至关重要，因此使nsP2成为开发VEEV治疗药物的极具吸引力的靶点。VEEV nsP2的338个氨基酸的C末端区域已在大肠杆菌中过表达、纯化并结晶。晶体衍射分辨率超过2.5埃，属于正交空间群P2(1)2(1)2(1)。已获得适用于相位分析的同晶型重原子衍生物，构建完整结构模型的工作正在进行中。
