Assignment of the N-terminal domain of mouse cGAS

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dc.contributor.authorAucharova, Hanna
dc.contributor.authorLinser, Rasmus
dc.date.accessioned2026-01-20T12:51:20Z
dc.date.available2026-01-20T12:51:20Z
dc.date.issued2025-01-04
dc.description.abstractCyclic GMP-AMP synthase (cGAS) is a DNA-sensing enzyme that is a member of the nucleotidyltransferase (NTase) family and functions as a DNA sensor. The protein is comprised of a catalytic NTase core domain and an unstructured hypervariable N-terminal domain (NTD) that was reported to increase protein activity by providing an additional DNA-binding surface. We report nearly complete 1H, 15N, and 13C backbone chemical-shift assignments of mouse cGAS NTD (residues 5-146), obtained with a set of 3D and 4D solution NMR experiments. Analysis of the chemical-shift values confirms that the NTD is intrinsically disordered. These resonance assignments can provide the basis for further studies such as activation by DNA and protein-protein interactions.en
dc.identifier.urihttp://hdl.handle.net/2003/44691
dc.language.isoen
dc.relation.ispartofseriesBiomolecular NMR assignments; 19(1)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectCyclic GMP-AMP synthaseen
dc.subjectcGASen
dc.subjectIntrinsically disordered proteinsen
dc.subjectIDPsen
dc.subjectNMR spectroscopyen
dc.subject.ddc540
dc.titleAssignment of the N-terminal domain of mouse cGASen
dc.typeText
dc.type.publicationtypeArticle
dcterms.accessRightsopen access
eldorado.dnb.deposittrue
eldorado.doi.registerfalse
eldorado.openaire.projectidentifierinfo:eu-repo/grantAgreement/EC/HE/101082494/EU/Fast-MAS Solid-State NMR as a Bypass to High-Molecular-Weight Proteins in Solution/bypassNMR/
eldorado.secondarypublicationtrue
eldorado.secondarypublication.primarycitationAucharova, H., Linser, R. Assignment of the N-terminal domain of mouse cGAS. Biomol NMR Assign 19, 35–39 (2025). https://doi.org/10.1007/s12104-024-10213-2
eldorado.secondarypublication.primaryidentifierhttps://doi.org/10.1007/s12104-024-10213-2

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Physikalische Chemie