Architecture et Fonction des Macromolécules Biologiques, Universités d'Aix-Marseille I et II, Marseille, France.
Adv Exp Med Biol. 2012;725:126-41. doi: 10.1007/978-1-4614-0659-4_8.
In this chapter, I focus on the biochemical and structural characterization of the complex between the intrinsically disordered C-terminal domain of the measles virus nucleoprotein (N(TAIL)) and the C-terminal X domain (XD) of the viral phosphoprotein (P). I summarize the main experimental data available so far pointing out the prevalently disordered nature of N(TAIL) even after complex formation and the role of the flexible C-terminal appendage in the binding reaction. I finally discuss the possible functional role of these residual disordered regions within the complex in terms of their ability to capture other regulatory, binding partners.
在这一章中，我专注于麻疹病毒核蛋白（N(TAIL)）的无规则结构域的 C 端与病毒磷蛋白（P）的 C 端 X 结构域（XD）之间复合物的生化和结构特征。我总结了到目前为止可用的主要实验数据，指出即使在复合物形成后，N(TAIL)的无规则结构性质仍然占主导地位，并且柔性 C 端附属物在结合反应中的作用。最后，我根据这些无规则结构域在复合物中捕获其他调节性、结合伙伴的能力，讨论了它们在复合物中可能的功能作用。
