Univ. Grenoble Alpes, CNRS, CEA, IBS, 38000, Grenoble, France.
Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt, Germany.
Biomol NMR Assign. 2021 Apr;15(1):173-176. doi: 10.1007/s12104-020-10001-8. Epub 2021 Jan 21.
The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the international covid19-nmr consortium, which aims to characterize SARS-CoV-2 proteins and RNAs, providing for example NMR chemical shift assignments of the different viral components. Our assignment will provide the basis for the identification of inhibitors and further functional and interaction studies of this essential protein.
来自 SARS-CoV-2 的非结构蛋白 nsp3 在病毒复制转录复合物中发挥着重要作用。Nsp3a 构成了 nsp3 的 N 端结构域，包含一个泛素样折叠结构域和一个无序的酸性链。nsp3a 的这一区域与病毒核蛋白和双层膜囊泡的结构有关。在这里，我们报告了 nsp3a 的两个结构域的骨架共振分配。该研究是在国际 covid19-nmr 联盟的框架内进行的，该联盟旨在对 SARS-CoV-2 蛋白和 RNA 进行特征描述，例如为不同病毒成分提供 NMR 化学位移分配。我们的分配将为鉴定抑制剂以及进一步研究该必需蛋白的功能和相互作用提供基础。
