PROTEO and Department of Biochemistry and Microbiology, Pavillon C-E MARCHAND, Universite Laval, 1030 avenue de Medecine, Local 3255, Quebec, QC G1V 0A6, Canada.
Biochem Cell Biol. 2010 Apr;88(2):315-23. doi: 10.1139/o09-155.
The Core protein of hepatitis C virus is involved in several interactions other than the encapsidation of viral RNA. We recently proposed that this is related to the fact that the N-terminal half of this protein (C82) is an intrinsically unstructured protein (IUP) domain. IUP domains can adopt a secondary structure when they are interacting with another molecule, such as a nucleic acid or a protein. It is also possible to mimic these conditions by modifying the environment of the protein. We investigated the propensity of this protein to fold as a function of salt concentration, detergent, pH, and 2,2,2-trifluoro-ethanol (TFE); only the addition of TFE resulted in a structural change. The effect of TFE addition was studied by circular dichroism, structural, and dynamic data obtained by NMR. The data indicate that C82 can adopt an alpha-helical structure; this conformation is likely relevant to one of the functional roles of the HCV Core protein.
丙型肝炎病毒的核心蛋白参与了几种除了病毒 RNA 包裹之外的相互作用。我们最近提出，这与该蛋白的 N 端半段（C82）是一种固有无结构蛋白（IUP）结构域有关。当 IUP 结构域与另一种分子（如核酸或蛋白质）相互作用时，它可以采用二级结构。通过修饰蛋白质的环境也可以模拟这些条件。我们研究了该蛋白在盐浓度、去污剂、pH 和 2,2,2-三氟乙醇（TFE）存在下折叠的趋势；只有添加 TFE 才会导致结构发生变化。通过圆二色性、NMR 获得的结构和动态数据研究了 TFE 添加的效果。数据表明，C82 可以采用α-螺旋结构；这种构象可能与丙型肝炎病毒核心蛋白的一种功能作用有关。
