# Assignment of the N-terminal domain of mouse cGAS

## TL;DR

This study provides detailed chemical-shift assignments for the N-terminal domain of mouse cGAS, confirming it is intrinsically disordered.

## Contribution

The paper presents nearly complete backbone chemical-shift assignments for the mouse cGAS N-terminal domain using NMR.

## Key findings

- The N-terminal domain of mouse cGAS is intrinsically disordered.
- Chemical-shift assignments were obtained for residues 5-146 of the NTD.
- The data can support future studies on DNA activation and protein interactions.

## Abstract

Cyclic 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.