Zhang Yang-De, Li Hao, Liu Hui, Pan Yi-Feng
National Hepatobiliary and Enteric Surgery Research Center of The Ministry of Health, Xiangya Hospital, Central South University, Hunan Province, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt 2):93-5. doi: 10.1107/S1744309106055849. Epub 2007 Jan 17.
The rotavirus outer capsid spike protein VP4 is utilized in the process of rotavirus attachment to and membrane penetration of host cells. VP4 is cleaved by trypsin into two domains: VP8* and VP5*. The VP8* domain is implicated in initial interaction with sialic acid-containing cell-surface carbohydrates and triggers subsequent virus invasion. The VP8* domain from porcine OSU rotavirus was cloned and expressed in Escherichia coli. Different crystal forms (orthorhombic P2(1)2(1)2(1) and tetragonal P4(1)2(1)2) were harvested from two distinct crystallization conditions. Diffraction data have been collected to 2.65 and 2.2 A resolution and the VP8*(65-224) structure was determined by molecular replacement.
轮状病毒外衣壳刺突蛋白VP4在轮状病毒附着于宿主细胞并穿透细胞膜的过程中发挥作用。VP4被胰蛋白酶切割成两个结构域：VP8和VP5。VP8结构域参与与含唾液酸的细胞表面碳水化合物的初始相互作用，并引发随后的病毒入侵。猪OSU轮状病毒的VP8结构域在大肠杆菌中进行克隆和表达。从两种不同的结晶条件下收获了不同的晶体形式（正交P2(1)2(1)2(1)和四方P4(1)2(1)2）。已收集到分辨率为2.65 Å和2.2 Å的衍射数据，并通过分子置换确定了VP8*(65 - 224)的结构。
