Aucharova, HannaLinser, Rasmus2026-01-202026-01-202025-01-04http://hdl.handle.net/2003/44691Cyclic 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.enBiomolecular NMR assignments; 19(1)https://creativecommons.org/licenses/by/4.0/Cyclic GMP-AMP synthasecGASIntrinsically disordered proteinsIDPsNMR spectroscopy540Article