ArticleNature structural & molecular biology2020
Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers.
Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 242 papers.
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242 citing papers in PubMed, 416 citations in OpenAlex.
- Full-length SARS-CoV-2 envelope protein adopts an interfacial topology in lipid bilayers.Biochimica et biophysica acta. Biomembranes · 2026Article
- Structural Bases for the Unconventional Activity of a Viroporin Channel.Biochemistry · 2026Article
- Targeting SARS-CoV-2 Structural and Accessory Proteins: Emerging Opportunities for Small-Molecule Coronavirus Antivirals.Pharmaceutics · 2026Review
- Nuclear magnetic resonance of membrane proteins-Advances and opportunities.Current opinion in structural biology · 2026Review
- SARS-CoV-2 enhances lysosomal exocytosis and deacidifies lysosomes to facilitate viral release.mLife · 2026Article
- Pentameric Architecture of the SARS-CoV-2 Envelope Protein Revealed by SEC-MALS, Cryo-EM, and Molecular Dynamics.The journal of physical chemistry. B · 2026Article
- SARS-CoV-2 envelope protein mitochondrial localization reveals host metabolic disruption.The Journal of biological chemistry · 2026Article
- Phosphatidylinositol Interactions with the SARS-CoV-2 Envelope Protein Investigated by LipidBiochemistry · 2026Article
- Clustering of SARS-CoV-2 membrane proteins in lipid bilayer membranes.PLoS computational biology · 2026Article
- Preclinical development of a cross-protective β-SARS-CoV-2 virus-like particle vaccine adjuvanted with MF59.NPJ vaccines · 2026Article
- Conserved Transmembrane Asparagine Is Essential for the Ion-Conducting Structure and Dynamics of the SARS-CoV-2 Envelope Protein.Journal of the American Chemical Society · 2026Article
- Structural and Computational Insights into the Attenuated Innate Immune Recognition of the SARS-CoV-2 N15 Lineage, an Early-Pandemic Variant.Computational and structural biotechnology journal · 2026Article
- SARS-CoV-2-host and interactions: the dual roles of E3 ubiquitin ligases and ubiquitin-like modification mechanisms in viral infection.Frontiers in immunology · 2026Review
- C-terminus-outward orientation of SARS-CoV-2 envelope proteins on viral capsid enables a novel virus-cell interaction pathway.Frontiers in cellular and infection microbiology · 2026Article
- The Redesign of the Molecular Scaffold of Viral Ion Channel Blockers.Computational and structural biotechnology journal · 2026Article
- Beyond the Spike Glycoprotein: Mutational Signatures in SARS-CoV-2 Structural Proteins.Infectious disease reports · 2025Article
- Membrane Depth Measurements of E Protein byBiophysica · 2025Article
- Impact of anionic lipids on the energy landscape of conformational transition in anion exchanger 1 (AE1).Nature communications · 2025Article
- "Molecular Docking and Dynamic Studies of Amide Derivatives from Cinnamic Acid with Potential Anti-Dengue Virus Activity".ChemistryOpen · 2025Article
- Article
182 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
An essential protein of the SARS-CoV-2 virus, the envelope protein E, forms a homopentameric cation channel that is important for virus pathogenicity. Here we report a 2.1-Å structure and the drug-binding site of E's transmembrane domain (ETM), determined using solid-state NMR spectroscopy. In lipid bilayers that mimic the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane, ETM forms a five-helix bundle surrounding a narrow pore. The protein deviates from the ideal α-helical geometry due to three phenylalanine residues, which stack within each helix and between helices. Together with valine and leucine interdigitation, these cause a dehydrated pore compared with the viroporins of influenza viruses and HIV. Hexamethylene amiloride binds the polar amino-terminal lumen, whereas acidic pH affects the carboxy-terminal conformation. Thus, the N- and C-terminal halves of this bipartite channel may interact with other viral and host proteins semi-independently. The structure sets the stage for designing E inhibitors as antiviral drugs.
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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.