7XXK

Crystal structure of SARS-CoV-2 N-CTD in complex with GMP

7XXK の概要

• エントリーDOI: 10.2210/pdb7xxk/pdb
• 分子名称: Nucleoprotein, THIOCYANATE ION, GUANOSINE-5'-MONOPHOSPHATE, ... (9 entities in total)
• 機能のキーワード: coronavirus, c-terminal domain, nucleocapsid, gmp, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 82685.08

構造登録者

Zhou, R.J.,Ni, X.C.,Lei, J. (登録日: 2022-05-30, 公開日: 2022-06-29, 最終更新日: 2024-11-13)

主引用文献

Ni, X.,Han, Y.,Yu, J.,Zhou, R.,Lei, J.
Structural basis of the C-terminal domain of SARS-CoV-2 N protein in complex with GMP reveals critical residues for RNA interaction.
Bioorg.Med.Chem.Lett., :130014-130014, 2024

PubMed Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein performs multiple functions during the viral life cycle, particularly in binding to the viral genomic RNA to form a helical ribonucleoprotein complex. Here, we present that the C-terminal domain of SARS-CoV-2 N protein (N-CTD) specifically interacts with polyguanylic acid (poly(G)). The crystal structure of the N-CTD in complex with 5'-guanylic acid (GMP, also known as guanosine monophosphate) was determined at a resolution of approximately 2.0 Å. A novel GMP-binding pocket in the N-CTD was illustrated. Residues Arg259 and Lys338 were identified to play key roles in binding to GMP through mutational analysis. These two residues are absolutely conserved in the other two highly pathogenic CoVs, SARS-CoV and Middle East respiratory syndrome coronavirus (MERS-CoV). Overall, our findings expand the structural information on N protein interacting with guanylate and reveal a conserved GMP-binding pocket as a potential antiviral target.

PubMed: 39489230
DOI: 10.1016/j.bmcl.2024.130014

実験手法

X-RAY DIFFRACTION (2 Å)