{"entity": "journal", "iuid": "611d33a699554fbea508eae4fb4681ae", "timestamp": "2026-03-16T18:43:52.955Z", "links": {"self": {"href": "https://publications.scilifelab.se/journal/Nucleosides%20Nucleotides%20Nucleic%20Acids.json"}, "display": {"href": "https://publications.scilifelab.se/journal/Nucleosides%20Nucleotides%20Nucleic%20Acids"}}, "title": "Nucleosides Nucleotides Nucleic Acids", "issn": "1532-2335", "issn-l": null, "publications_count": 1, "publications": [{"entity": "publication", "iuid": "3a1bfb1e41aa466b98cdc7bf1ab88abb", "links": {"self": {"href": "https://publications.scilifelab.se/publication/3a1bfb1e41aa466b98cdc7bf1ab88abb.json"}, "display": {"href": "https://publications.scilifelab.se/publication/3a1bfb1e41aa466b98cdc7bf1ab88abb"}}, "title": "New insights into complex formation by SARS-CoV-2 nsp10 and nsp14.", "authors": [{"family": "Sele", "given": "C\u00e9leste", "initials": "C"}, {"family": "Krupinska", "given": "Ewa", "initials": "E"}, {"family": "Andersson Rasmussen", "given": "Anna", "initials": "A"}, {"family": "Ekstr\u00f6m", "given": "Simon", "initials": "S"}, {"family": "Hultgren", "given": "Lucas", "initials": "L"}, {"family": "Lou", "given": "Jiaqi", "initials": "J"}, {"family": "Kozielski", "given": "Frank", "initials": "F"}, {"family": "Fisher", "given": "S Zo\u00eb", "initials": "SZ"}, {"family": "Knecht", "given": "Wolfgang", "initials": "W"}], "type": "journal article", "published": "2024-02-29", "journal": {"title": "Nucleosides Nucleotides Nucleic Acids", "issn": "1532-2335", "pages": "1-15", "issn-l": null}, "abstract": "SARS-CoV-2 non-structural protein 10 (nsp10) is essential for the stimulation of enzymatic activities of nsp14 and nsp16, acting as both an activator and scaffolding protein. Nsp14 is a bifunctional enzyme with the N-terminus containing a 3'-5' exoribonuclease (ExoN) domain that allows the excision of nucleotide mismatches at the virus RNA 3'-end, and a C-terminal N7-methyltransferase (N7-MTase) domain. Nsp10 is required for stimulating both ExoN proofreading and the nsp16 2'-O-methyltransferase activities. This makes nsp10 a central player in both viral resistance to nucleoside-based drugs and the RNA cap methylation machinery that helps the virus evade innate immunity. We characterised the interactions between full-length nsp10 (139 residues), N- and C-termini truncated nsp10 (residues 10-133), and nsp10 with a C-terminal truncation (residues 1-133) with nsp14 using microscale thermophoresis, multi-detection SEC, and hydrogen-deuterium (H/D) exchange mass spectrometry. We describe the functional role of the C-terminal region of nsp10 for binding to nsp14 and show that full N- and C-termini of nsp10 are important for optimal binding. In addition, our H/D exchange experiments suggest an intermediary interaction of nsp10 with the N7-MTase domain of nsp14. In summary, our results suggest intermediary steps in the process of association or dissociation of the nsp10-nsp14 complex, involving contacts between the two proteins in regions not identifiable by X-ray crystallography alone.", "doi": "10.1080/15257770.2024.2321600", "pmid": "38422227", "labels": {"Structural Proteomics": "Service"}, "xrefs": [], "notes": [], "created": "2024-03-01T08:16:19.543Z", "modified": "2024-03-01T08:16:19.718Z"}], "created": "2024-03-01T08:16:19.552Z", "modified": "2024-03-01T08:16:19.552Z"}