ArticleCurrent research in virological science2021
SARS-CoV-2 NSP1 C-terminal (residues 131-180) is an intrinsically disordered region in isolation.
Article in Current research in virological science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- The role of intrinsically disordered regions of SARS-CoV-2 nucleocapsid and non-structural protein 1 proteins.Frontiers in chemistry · 2025Review
- Structure-function mapping and mechanistic insights on the SARS CoV2 Nsp1.Protein science : a publication of the Protein Society · 2024Article
- SARS-CoV2 Nsp1 is a metal-dependent DNA and RNA endonuclease.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Coronavirus takeover of host cell translation and intracellular antiviral response: a molecular perspective.The EMBO journal · 2024Review
- Antiviral responses versus virus-induced cellular shutoff: a game of thrones between influenza A virus NS1 and SARS-CoV-2 Nsp1.Frontiers in cellular and infection microbiology · 2024Review
- Two Ligand-Binding Sites on SARS-CoV-2 Non-Structural Protein 1 Revealed by Fragment-Based X-ray Screening.International journal of molecular sciences · 2022Article
- Viral and cellular translation during SARS-CoV-2 infection.FEBS open bio · 2022Review
- Melatonin: Regulation of Viral Phase Separation and Epitranscriptomics in Post-Acute Sequelae of COVID-19.International journal of molecular sciences · 2022Review
- Clinically observed deletions in SARS-CoV-2 Nsp1 affect its stability and ability to inhibit translation.FEBS letters · 2022Article
- Mitoxantrone dihydrochloride, an FDA approved drug, binds with SARS-CoV-2 NSP1 C-terminal.RSC advances · 2022Article
- Extended ensemble simulations of a SARS-CoV-2 nsp1-5'-UTR complex.PLoS computational biology · 2022Article
- Transactivation domain of Adenovirus Early Region 1A (E1A): Investigating folding dynamics and aggregation.Current research in structural biology · 2022Article
- Article
- Investigating the conformational dynamics of SARS-CoV-2 NSP6 protein with emphasis on non-transmembrane 91-112 & 231-290 regions.Microbial pathogenesis · 2021Article
- Conformational dynamics of 13 amino acids long NSP11 of SARS-CoV-2 under membrane mimetics and different solvent conditions.Microbial pathogenesis · 2021Article
- Modelling studies reveal the importance of the C-terminal inter motif loop of NSP1 as a promising target site for drug discovery and screening of potential phytochemicals to combat SARS-CoV-2.Journal of molecular graphics & modelling · 2021Article
- Coronavirus Nsp1: Immune Response Suppression and Protein Expression Inhibition.Frontiers in microbiology · 2021Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NSP1- C terminal structure in complex with ribosome using cryo-EM is available now, and the N-terminal region structure in isolation is also deciphered in literature. However, as a reductionist approach, the conformation of NSP1- C terminal region (NSP1-CTR; amino acids 131-180) has not been studied in isolation. We found that NSP1-CTR conformation is disordered in an aqueous solution. Further, we examined the conformational propensity towards alpha-helical structure using trifluoroethanol, we observed induction of helical structure conformation using CD spectroscopy. Additionally, in SDS, NSP1-CTR shows a conformational change from disordered to ordered, possibly gaining alpha-helix in part. But in the presence of neutral lipid DOPC, a slight change in conformation is observed, which implies the possible role of hydrophobic interaction and electrostatic interaction on the conformational changes of NSP1. Fluorescence-based studies have shown a blue shift and fluorescence quenching in the presence of SDS, TFE, and lipid vesicles. In agreement with these results, fluorescence lifetime and fluorescence anisotropy decay suggest a change in conformational dynamics. The zeta potential studies further validated that the conformational dynamics are primarily because of hydrophobic interaction. These experimental studies were complemented through Molecular Dynamics (MD) simulations, which have shown a good correlation and testifies our experiments. We believe that the intrinsically disordered nature of the NSP1-CTR will have implications for enhanced molecular recognition feature properties of this IDR, which may add disorder to order transition and disorder-based binding promiscuity with its interacting proteins.
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