Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3.

Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3.
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DOI:
10.1007/s12104-021-10059-y
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发表时间:
2022-04
影响因子:
0.9
通讯作者:
Hoch JC
Hoch JC
中科院分区:
生物学4区
文献类型:
--
作者:
Pustovalova Y;Gorbatyuk O;Li Y;Hao B;Hoch JC

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全球COVID-19大流行由严重急性呼吸道综合征冠状病毒2(SARS-CoV-2)引起。非结构蛋白3(nonstructural protein 3,nsp 3)是SARS冠状病毒2型编码的最大蛋白质,由1945个氨基酸残基组成。它由十几个独立的域组成,具有各种功能。在早期爆发后,在密切相关的SARS冠状病毒中研究了其中许多结构域。尽管如此,含有两个跨膜和三个膜外结构域的nsp 3的C-末端区域的结构和功能信息仍然不完整。这部分蛋白质似乎参与了双膜囊泡(DMV)形成的启动,DMV是病毒构建的膜细胞器,用于隐藏其复制-转录复合物以免受宿主免疫防御。在这里,我们提出了几乎完整的骨架和Ile,Leu,和瓦尔甲基化学位移分配的最C-末端结构域的nsp 3,CoV-Y。由于CoV-Y的确切功能和结合伴侣仍然未知,我们的数据为未来蛋白质-蛋白质相互作用的NMR研究提供了基础,以阐明DMV形成的分子机制。
The worldwide COVID-19 pandemic is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Nonstructural protein 3 (nsp3) has 1945 residues and is the largest protein encoded by SARS-CoV-2. It comprises more than a dozen independent domains with various functions. Many of these domains were studied in the closely-related virus SARS-CoV following an earlier outbreak. Nonetheless structural and functional information on the C-terminal region of nsp3 containing two transmembrane and three extra-membrane domains remains incomplete. This part of the protein appears to be involved in initiation of double membrane vesicle (DMV) formation, membranous organelles the virus builds to hide its replication-transcription complex from host immune defenses. Here we present the near-complete backbone and Ile, Leu, and Val methyl group chemical shift assignments of the most C-terminal domain of nsp3, CoV-Y. As the exact function and binding partners of CoV-Y remain unknown, our data provide a basis for future NMR studies of protein–protein interactions to elucidate the molecular mechanism of DMV formation.
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