Fig. 7: Dimerization prepares PARP15 for target engagement by stabilizing distinct surface loops.
From: Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15
Working model of PARP15 activation based on the data presented in this study: ART domain dimerization and NAD+ binding together bring surface loops into position for engagement of target protein and transfer of ADP-ribose. Both monomer and dimer can bind NAD+ but dimerization promotes NAD+ binding. Kd values for ART domain dimerization and dinucleotide binding are from our experiments detailed in Fig. 1 and Supplementary Fig. 8 (values for EB-47), respectively.
