SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study
Severe acute respiratory syndrome virus 2 (SARS-CoV-2) belongs to the single-stranded positive-sense RNA family. The virus contains a large genome that encodes four structural proteins, small envelope (E), matrix (M), nucleocapsid phosphoprotein (N), spike (S), and 16 nonstructural proteins (nsp1-16) that together, ensure replication of the virus in the host cell. Among these proteins, the interactions of N and Nsp3 are essential that links the viral genome for processing. The N proteins reside at CoV RNA synthesis sites known as the replication–transcription complexes (RTCs). The N-terminal of N has RNA-binding domain (N-NTD), capturing the RNA genome while the C-terminal domain (N-CTD) anchors the viral Nsp3, a component of RTCs. Although the structural information has been recently released, the residues involved in contacts between N-CTD with Nsp3 are still unknown. To find the residues involved in interactions between two proteins, three-dimensional structures of both proteins were retrieved and docked using HADDOCK. Residues at N-CTD were detected in interaction with L499, R500, K501, V502, P503, T504, D505, N506, Y507, I508, T509, K529, K530K532, S533 of Nsp3 and N-NTD to synthesize SARS-CoV-2 RNA. The interaction between Nsp3 and CTD of N protein may be a potential drug target. The current study provides information for better understanding the interaction between N protein and Nsp3 that could be a possible target for future inhibitors. Graphic abstract.
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Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:203 |
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| Enthalten in: |
Archives of microbiology - 203(2020), 1 vom: 04. Aug., Seite 59-66 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Khan, Muhammad Tahir [VerfasserIn] |
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| Links: |
Volltext [lizenzpflichtig] |
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© Springer-Verlag GmbH Germany, part of Springer Nature 2020 |
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| doi: |
10.1007/s00203-020-01998-6 |
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| 520 | |a Severe acute respiratory syndrome virus 2 (SARS-CoV-2) belongs to the single-stranded positive-sense RNA family. The virus contains a large genome that encodes four structural proteins, small envelope (E), matrix (M), nucleocapsid phosphoprotein (N), spike (S), and 16 nonstructural proteins (nsp1-16) that together, ensure replication of the virus in the host cell. Among these proteins, the interactions of N and Nsp3 are essential that links the viral genome for processing. The N proteins reside at CoV RNA synthesis sites known as the replication–transcription complexes (RTCs). The N-terminal of N has RNA-binding domain (N-NTD), capturing the RNA genome while the C-terminal domain (N-CTD) anchors the viral Nsp3, a component of RTCs. Although the structural information has been recently released, the residues involved in contacts between N-CTD with Nsp3 are still unknown. To find the residues involved in interactions between two proteins, three-dimensional structures of both proteins were retrieved and docked using HADDOCK. Residues at N-CTD were detected in interaction with L499, R500, K501, V502, P503, T504, D505, N506, Y507, I508, T509, K529, K530K532, S533 of Nsp3 and N-NTD to synthesize SARS-CoV-2 RNA. The interaction between Nsp3 and CTD of N protein may be a potential drug target. The current study provides information for better understanding the interaction between N protein and Nsp3 that could be a possible target for future inhibitors. Graphic abstract | ||
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| 700 | 1 | |a Zeb, Muhammad Tariq |4 aut | |
| 700 | 1 | |a Ahsan, Hina |4 aut | |
| 700 | 1 | |a Ahmed, Abrar |4 aut | |
| 700 | 1 | |a Ali, Arif |4 aut | |
| 700 | 1 | |a Akhtar, Khalid |4 aut | |
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| 700 | 1 | |a Khan, Anwar Sheed |4 aut | |
| 700 | 1 | |a Ahmad, Manzoor |4 aut | |
| 700 | 1 | |a Wei, Dong-Qing |4 aut | |
| 700 | 1 | |a Irfan, Muhammad |0 (orcid)0000-0002-1060-4436 |4 aut | |
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