1H, 15N and 13C resonance assignments of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus
1H, 15N and 13C resonance assignments of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus
复制标题
狂犬病病毒西原株P蛋白C末端结构域的1H、15N和13C共振分配
DOI：
10.1007/s12104-018-9841-4
复制
发表时间：
2018
影响因子：
0.9
通讯作者：
Gooley Paul R.
中科院分区：
文献类型：
--
作者：
Zhan Jingyu;Hossain Md. Alamgir;Sethi Ashish;Ose Toyoyuki;Moseley Gregory W.;Gooley Paul R.
狂犬病病毒P蛋白的C末端结构域是一个多功能结构域，既能与病毒蛋白相互作用，又能与宿主细胞蛋白相互作用。在这里，我们报告了狂犬病病毒西贺株P蛋白这个结构域的1H、13C和15N化学位移指定，狂犬病病毒西贺株是一个致病的实验室毒株，很好地研究了狂犬病病毒蛋白的毒力功能，包括P蛋白。数据和二级结构分析与报道的狂犬病CVS株相同结构域的主要螺旋结构很好地一致，通过结晶学解决。这些任务将使未来的解决方案研究P蛋白与病毒和宿主蛋白的相互作用，以及翻译后修饰的影响。
The C-terminal domain of the P protein of rabies virus is a multifunctional domain that interacts with both viral and host cell proteins. Here we report the1H,13C and15N chemical shift assignments of this domain from P protein of theNishigaharastrain of rabies virus, a pathogenic laboratory strain well established for studies of virulence functions of rabies virus proteins, including P protein. The data and secondary structure analysis are in good agreement with the reported predominantly helical structure of the same domain from the CVS strain of rabies solved by crystallography. These assignments will enable future solution studies of the interactions of the P protein with viral and host proteins, and the effects of post-translational modifications.