SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study.

SARS-CoV-2 nucleocapsid and Nsp3 binding: an in silico study. Arch Microbiol. 2020 Aug 04;: Authors: Khan MT, Zeb MT, Ahsan H, Ahmed A, Ali A, Akhtar K, Malik SI, Cui Z, Ali S, Khan AS, Ahmad M, Wei DQ, Irfan M Abstract 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 interact...
Source: Archives of Microbiology - Category: Microbiology Authors: Tags: Arch Microbiol Source Type: research