1H, 13C and 15N resonance assignments of the N-terminal intrinsically disordered region and WGR domain of human PARP2

Abstract

Poly(ADP-ribose) polymerase 2 (PARP2) is a key sensor of DNA single-strand breaks that catalyzes ADP-ribosylation of itself and other substrates to initiate DNA repair. Human PARP2 contains an intrinsically disordered N-terminal domain (NTD) that mediates chromatin association and nuclear localization, a central WGR domain that recognizes DNA breaks, and a catalytic domain responsible for poly(ADP-ribose) synthesis. Despite its importance in genome maintenance and as a target of clinical PARP inhibitors, detailed information on the structural and dynamic properties of the NTD and WGR domains has remained limited. Here, we report the ¹H, ¹³C, and ¹⁵N resonance assignments of the N-terminal intrinsically disordered region (residues 1–89) and the WGR domain (residues 90–212) of human PARP2. Resonance assignments were first obtained separately for each domain and subsequently transferred to a combined NTD–WGR construct. These assignments provide a foundation for future studies investigating the conformational dynamics, DNA recognition mechanisms, and allosteric regulation of PARP2 in chromatin and repair signaling.