Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9

被引：8

作者：

F. Dudas, Erika ^{[1
]}

Puglisi, Rita ^{[1
]}

Korn, Sophie Marianne ^{[2
,3
]}

Alfano, Caterina ^{[4
]}

Bellone, Maria Laura ^{[5
]}

Piaz, Fabrizio Dal ^{[5
]}

Kelly, Geoff ^{[6
]}

Monaca, Elisa ^{[4
]}

Schlundt, Andreas ^{[2
,3
]}

Schwalbe, Harald ^{[2
,3
]}

Pastore, Annalisa ^{[1
]}

机构：

[1] Kings Coll London, Maurice Wohl Inst, Dept Basic & Clin Neurosci, UK DRI, 5 Cutcombe Rd, London SE5 9RT, England

[2] Goethe Univ Frankfurt, Inst Mol Biosci, Max von Laue Str 9, D-60438 Frankfurt M, Germany

[3] Goethe Univ Frankfurt, Inst Organ Chem & Chem Biol, Ctr Biomol Magnet Resonance BMRZ, Max von Laue Str 7, D-60438 Frankfurt M, Germany

[4] Fdn Ri Med, I-90133 Palermo, Italy

[5] Univ Salerno, Dept Med & Surg, Via Giovanni Paolo II, I-84081 Baronissi, SA, Italy

[6] MRC Biomed NMR Ctr, Francis Crick Inst, 1 Midland Rd, London NW1 1AT, England

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2021年 / 15卷 / 02期

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

Coronavirus; Covid-19; NMR; Protein; SARS-CoV-2; Solution NMR; Structure; DOMAIN;

D O I：

10.1007/s12104-021-10011-0

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

As part of an International consortium aiming at the characterization by NMR of the proteins of the SARS-CoV-2 virus, we have obtained the virtually complete assignment of the backbone atoms of the non-structural protein nsp9. This small (12 kDa) protein is encoded by ORF1a, binds to RNA and seems to be essential for viral RNA synthesis. The crystal structures of the SARS-CoV-2 protein and other homologues suggest that the protein is dimeric as also confirmed by analytical ultracentrifugation and dynamic light scattering. Our data constitute the prerequisite for further NMR-based characterization, and provide the starting point for the identification of small molecule lead compounds that could interfere with RNA binding and prevent viral replication.

引用

页码：235 / 241

页数：7

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