{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hernandez G"],"funding":["SR&TD","PPBI","European EC Horizon 2020","MOSTMICRO FCT","COMPETE 2020","FCT","Foundation for Science and Technology","FEDER","SR&TD","PT-NMR FCT","LS4FUTURE"],"pagination":["gkaf502"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12159747"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(11)"],"pubmed_abstract":["The SARS-CoV-2 nucleocapsid (N) protein is essential for the viral life cycle, facilitating RNA packaging, replication, and host-cell interactions. Its ability to self-assemble and undergo phase separation is critical for these functions but remains poorly understood. Using an integrated approach combining small-angle X-ray scattering (SAXS), nuclear magnetic resonance spectroscopy, computational modeling, and biophysical assays, we uncover key mechanisms underpinning N-protein's dynamic self-assembly. We show that the N-protein's interdomain linker (IDL) contains a conserved coiled-coil (CC) motif that drives transient interactions between protein subunits, enabling the formation of progressively larger complexes at higher concentrations. SAXS analysis and ensemble modeling reveal that th"],"journal":["Nucleic acids research"],"pubmed_title":["Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation."],"pmcid":["PMC12159747"],"funding_grant_id":["CEECIND/01443/2017","UIDP/04612/2020","PD/BD/147227/2019","UIDB/04612/2020","810856","PTDC/BIA-BFS/0391/2021","0145-FEDER-007660","LA/P/0087/2020","UI/BD/154576/2022","01/SAICT/2016"],"pubmed_authors":["Hernandez G","Gomes T","Veloso T","Cordeiro TN","Lopes J","Fernandes NP","Martins ML"],"additional_accession":[]},"is_claimable":false,"name":"Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation.","description":"The SARS-CoV-2 nucleocapsid (N) protein is essential for the viral life cycle, facilitating RNA packaging, replication, and host-cell interactions. Its ability to self-assemble and undergo phase separation is critical for these functions but remains poorly understood. Using an integrated approach combining small-angle X-ray scattering (SAXS), nuclear magnetic resonance spectroscopy, computational modeling, and biophysical assays, we uncover key mechanisms underpinning N-protein's dynamic self-assembly. We show that the N-protein's interdomain linker (IDL) contains a conserved coiled-coil (CC) motif that drives transient interactions between protein subunits, enabling the formation of progressively larger complexes at higher concentrations. SAXS analysis and ensemble modeling reveal that th","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-03T07:31:01.5Z","creation":"2026-04-26T03:09:26.818Z"},"accession":"S-EPMC12159747","cross_references":{"pubmed":["40503686"],"doi":["10.1093/nar/gkaf502"]}}