ArticleStructure (London, England : 1993)2019
MORC3 Is a Target of the Influenza A Viral Protein NS1.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Nonstructural Protein 1 of Influenza A (NS1A) Demonstrates Strain-Specific dsRNA Binding Capabilities.ACS infectious diseases · 2025Article
- Structural Investigations of Interactions between the Influenza a Virus NS1 and Host Cellular Proteins.Viruses · 2023Review
- Non-histone binding functions of PHD fingers.Trends in biochemical sciences · 2023Review
- Vital for Viruses: Intrinsically Disordered Proteins.Journal of molecular biology · 2023Review
- Antiviral effects of interferon-stimulated genes in bats.Frontiers in cellular and infection microbiology · 2023Review
- Article
- Mechanistic similarities in recognition of histone tails and DNA by epigenetic readers.Current opinion in structural biology · 2021Review
- Morc3 silences endogenous retroviruses by enabling Daxx-mediated histone H3.3 incorporation.Nature communications · 2021Article
- Histone H3 N-terminal mimicry drives a novel network of methyl-effector interactions.The Biochemical journal · 2021Article
- Molecular mechanism of the MORC4 ATPase activation.Nature communications · 2020Article
- MORC3 Forms Nuclear Condensates through Phase Separation.iScience · 2019Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Microrchidia 3 (MORC3), a human ATPase linked to several autoimmune disorders, has been characterized both as a negative and positive regulator of influenza A virus. Here, we report that the CW domain of MORC3 (MORC3-CW) is targeted by the C-terminal tail of the influenza H3N2 protein NS1. The crystal structure of the MORC3-CW:NS1 complex shows that NS1 occupies the same binding site in CW that is normally occupied by histone H3, a physiological ligand of MORC3-CW. Comparable binding affinities of MORC3-CW to H3 and NS1 peptides and to the adjacent catalytic ATPase domain suggest that the viral protein can compete with the host histone for the association with CW, releasing MORC3 autoinhibition and activating the catalytic function of MORC3. Our structural, biochemical, and cellular analyses suggest that MORC3 might affect the infectivity of influenza virus and therefore has a role in cell immune response.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.