1H, 15N, and 13C resonance assignments of the N-terminal domain and ser-arg-rich intrinsically disordered region of the nucleocapsid protein of the SARS-CoV-2

被引:0
|
作者
Bezerra, Peter R. [1 ,2 ]
Vasconcelos, Ariana A. [1 ,2 ]
Almeida, Vitor S. [1 ,2 ]
Neves-Martins, Thais C. [1 ]
Mebus-Antunes, Nathane C. [1 ]
Almeida, Fabio C. L. [1 ,2 ]
机构
[1] Univ Fed Rio de Janeiro, Natl Ctr Nucl Magnet Resonance, Inst Med Biochem IBqM, Rio De Janeiro, RJ, Brazil
[2] Univ Fed Rio de Janeiro, Natl Ctr Nucl Magnet Resonance CNRMN, Natl Ctr Struct Biol & Bioimaging CENABIO, BR-21941902 Rio De Janeiro, Brazil
关键词
N protein; NMR; Sars-CoV-2; IDR; SR-rich; REGULATORY SEQUENCE TRS; NMR;
D O I
10.1007/s12104-024-10191-5
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The nucleocapsid (N) protein of SARS-CoV-2 is a multifunctional protein involved in nucleocapsid assembly and various regulatory functions. It is the most abundant protein during viral infection. Its functionality is closely related to its structure, which comprises two globular domains, the N-terminal domain (NTD) and the C-terminal domain (CTD), flanked by intrinsically disordered regions. The linker between the NTD and CTD includes a Serine-Arginine rich (SR) region, which is crucial for the regulation of the N protein's function. Here, we report the near-complete assignment of the construct containing the NTD followed by the SR region (NTD-SR). Additionally, we describe the dynamic nature of the SR region and compare it with all other available chemical shift assignments reported for the SR region.
引用
收藏
页码:219 / 225
页数:7
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