SARS CoV 2核体蛋白的二元化域作为单体部分失序,形成一个高亲和力动态复合体
Jasmine Cubuk1,2, J Jeremias Incicco1,3, Kathleen B Hall1
1Department of Biochemistry and Molecular Biophysics, Washington University in St Louis, 660 Euclid Ave, 63110, Saint Louis, MO, USA.
bioRxiv : the preprint server for biology
|October 10, 2024
概括
在SARS-CoV-2核囊蛋白质.
科学领域:
- 结构生物学是结构生物学.
- 病毒学 病毒学
- 生物物理学的生物物理.
背景情况:
- 作为病毒的关键组成部分,SARS-CoV-2核体 (N) 蛋白对于包装病毒基因组至关重要.
- 蛋白质-蛋白质和蛋白质-RNA相互作用调解了基因组紧缩,N蛋白自我关联增加了它的功能价值.
研究的目的:
- 量化控制SARS-CoV-2 N蛋白质二极体形成的机制.
- 为了研究N蛋白质二元化领域的结构动态和能量.
主要方法:
- 单分子弗斯特共振能量转移 (smFRET) 用于研究蛋白质构造和相互作用.
- 使用热力学分析来确定解离常数和二分化驱动力.
主要成果:
- 单体N蛋白质二元化域存在于扩展的,动态的配置.
- 蛋白质添加稳定了折叠的二分体,具有高的转移效率,表明在23°C时离合常数约为12nM.
- 模量化是通过合折叠和结合进行合驱动的,而模量体保留了一些形状灵活性.
结论:
- 单质N蛋白固有的灵活性对于形成相互锁定的二元结构至关重要.
- 在二分体中保持灵活性可能会促进RNA结合,并影响病毒相分离特性.
- 温度依赖的二分化可能解释了N蛋白相分离行为的观察到的变化.
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