SARS-CoV-2 核苷酸蛋白 N 端结构域和富含 ser-arg 的内在无序区的 1H、15N 和 13C 共振赋值。

IF 0.8 4区 生物学 Q4 BIOPHYSICS
Peter R. Bezerra, Ariana A. Vasconcelos, Vitor S. Almeida, Thais C. Neves-Martins, Nathane C. Mebus-Antunes, Fabio C. L. Almeida
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引用次数: 0

摘要

SARS-CoV-2 的核苷酸蛋白(N)是一种多功能蛋白,参与核苷酸组装和各种调控功能。它是病毒感染过程中含量最高的蛋白质。它的功能与其结构密切相关,包括两个球状结构域,即 N-末端结构域(NTD)和 C-末端结构域(CTD),两侧是内在无序区。NTD和CTD之间的连接区包括一个富含丝氨酸-精氨酸(SR)的区域,该区域对调控N蛋白的功能至关重要。在这里,我们报告了包含 NTD 和 SR 区(NTD-SR)的构建体的近乎完整的分配。此外,我们还描述了 SR 区域的动态性质,并将其与所有其他已报道的 SR 区域的化学位移赋值进行了比较。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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

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

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.

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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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