ArticleProtein science : a publication of the Protein Society2022
CTD of SARS-CoV-2 N protein is a cryptic domain for binding ATP and nucleic acid that interplay in modulating phase separation.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- A ComprehensiveAngewandte Chemie (International ed. in English) · 2026Article
- The regulatory mechanisms of SARS-CoV-2 N protein helicase and its annealing activity.iScience · 2025Article
- Review
- In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate.International journal of molecular sciences · 2024Review
- SARS-CoV-2 nucleocapsid protein interaction with YBX1 displays oncolytic properties through PKM mRNA destabilization.Molecular cancer · 2024Article
- Assembly of SARS-CoV-2 nucleocapsid protein with nucleic acid.Nucleic acids research · 2024Article
- Molecular Mechanisms and Potential Antiviral Strategies of Liquid-Liquid Phase Separation during Coronavirus Infection.Biomolecules · 2024Review
- Adenosine Triphosphate: The Primordial Molecule That Controls Protein Homeostasis and Shapes the Genome-Proteome Interface.Biomolecules · 2024Review
- Aptamers targeting SARS-CoV-2 nucleocapsid protein exhibit potential anti pan-coronavirus activity.Signal transduction and targeted therapy · 2024Article
- Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.bioRxiv : the preprint server for biology · 2023Article
- RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid.PNAS nexus · 2023Article
- A hybrid structure determination approach to investigate the druggability of the nucleocapsid protein of SARS-CoV-2.Nucleic acids research · 2023Article
- Association of SARS-CoV-2 Nucleocapsid Protein Mutations with Patient Demographic and Clinical Characteristics during the Delta and Omicron Waves.Microorganisms · 2023Article
- Phase-separated nucleocapsid protein of SARS-CoV-2 suppresses cGAS-DNA recognition by disrupting cGAS-G3BP1 complex.Signal transduction and targeted therapy · 2023Article
- ATP and nucleic acids competitively modulate LLPS of the SARS-CoV2 nucleocapsid protein.Communications biology · 2023Article
- Nucleoside Analogs and Perylene Derivatives Modulate Phase Separation of SARS-CoV-2 N Protein and Genomic RNA In Vitro.International journal of molecular sciences · 2022Article
- Can iron, zinc, copper and selenium status be a prognostic determinant in COVID-19 patients?Environmental toxicology and pharmacology · 2022Review
- A review of the effects of ATP and hydroxychloroquine on the phase separation of the SARS-CoV-2 nucleocapsid protein.Biophysical reviews · 2022Review
- CTD of SARS-CoV-2 N protein is a cryptic domain for binding ATP and nucleic acid that interplay in modulating phase separation.Protein science : a publication of the Protein Society · 2022Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
SARS-CoV-2 nucleocapsid (N) protein plays essential roles in many steps of the viral life cycle, thus representing a key drug target. N protein contains the folded N-/C-terminal domains (NTD/CTD) and three intrinsically disordered regions, while its functions including liquid-liquid phase separation (LLPS) depend on the capacity in binding various viral/host-cell RNA/DNA of diverse sequences. Previously NTD was established to bind various RNA/DNA while CTD to dimerize/oligomerize for forming high-order structures. By NMR, here for the first time we decrypt that CTD is not only capable of binding S2m, a specific probe derived from SARS-CoV-2 gRNA but with the affinity even higher than that of NTD. Very unexpectedly, ATP, the universal energy currency for all living cells with high cellular concentrations (2-16 mM), specifically binds CTD with Kd of 1.49 ± 0.28 mM. Strikingly, the ATP-binding residues of NTD/CTD are identical in the SARS-CoV-2 variants while ATP and S2m interplay in binding NTD/CTD, as well as in modulating LLPS critical for the viral life cycle. Results together not only define CTD as a novel binding domain for ATP and nucleic acid, but enforce our previous proposal that ATP has been evolutionarily exploited by SARS-CoV-2 to complete its life cycle in the host cell. Most importantly, the unique ATP-binding pockets on NTD/CTD may offer promising targets for design of specific anti-SARS-CoV-2 molecules to fight the pandemic. Fundamentally, ATP emerges to act at mM as a cellular factor to control the interface between the host cell and virus lacking the ability to generate ATP.
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