Fig. 1: Binding of PARP1 versus DNA-bound PARP1 to phosphorylated Erk.
From: Signal-induced PARP1-Erk synergism mediates IEG expression
a A ribbon structural model for the open conformation of PARP1 with optional consensus docking sites for phosphorylated Erk. Erk2 monomers in a homodimer (formed after Erk2 phosphorylation) are indicated by dark and light gray ribbons. Optional Erk-binding motifs on the HD, WGR and the CAT domain of PARP1 are indicated by orange spheres. The CRS/CD protein-binding region on Erk2 and the optional Erk-binding motifs on PARP1 are highlighted by red and blue shadows, respectively (from ref. 20) b The modeled conformation of PARP1 bound to damaged DNA indicating the occluded docking sites of phosphorylated Erk (from Ref # 20). c Autoradiograms presenting a comparison between the dose-dependent [32P]poly-ADP-ribosylation of recombinant PARP1 bound to recombinant phosphorylated Erk2 and the dose-dependent [32P]poly-ADP-ribosylation of recombinant PARP1 bound to DNA with single strand breaks, (nicked DNA, nDNA). [32P]poly-ADP-ribosylation was achieved in a mixture of β-NAD and [32P]NAD at the indicated concentrations (from ref. 19)
