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Complex assembly, crystallization and preliminary X-ray crystallographic analysis of duck MHC class I complexed with a TUMV viral peptide.
Research in Veterinary Science ( IF 2.2 ) Pub Date : 2020-07-18 , DOI: 10.1016/j.rvsc.2020.07.009
Zixin Liu 1 , Xiaoli Xie 1 , Zhuolin Li 1 , Lin Zhang 2 , Nianzhi Zhang 1
Affiliation  

The CTL immune response mediated by MHC I plays an important role in duck anti-TMUV infection. This study reports the expression, purification and crystallization of a complex of duck MHC class I molecules Anpl-UAA*SD, duck β2-microglobulin (Anpl-β2m) and the polypeptide LRKRQLTVL (LRK9) derived from Tembusu virus (TMUV) NS3. The crystal diffraction resolution is 1.50 Å and belongs to the P62 space group, and the unit cell parameters are a = 82.468, b = 82.468, c = 112.507. The Matthew's constant is calculated to be 2.32 Å3 Da −1, and an asymmetric unit contains a complex molecule with a solvent content of 47%. The research lays the foundation for the structure of immune molecules about duck anti-TMUV research.



中文翻译:

鸭MHC I类与TUMV病毒肽复合的复合物组装,结晶和初步X射线晶体学分析。

MHC I介导的CTL免疫应答在鸭抗TMUV感染中起重要作用。这项研究报告了鸭MHC I类分子Anpl -UAA * SD,鸭β2-微球蛋白(Anpl - β2m)和衍生自Tembusu病毒(TMUV)NS3的多肽LRKRQLTVL(LRK9)的复合物的表达,纯化和结晶。晶体衍射分辨率为1.50,属于P 6 2空间群,晶胞参数为a  = 82.468,b  = 82.468,c  = 112.507。马修常数经计算为2.32埃3 沓-1,不对称单元包含溶剂含量为47%的复杂分子。该研究为鸭抗TMUV研究奠定了免疫分子结构的基础。

更新日期:2020-07-25
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