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. Author manuscript; available in PMC: 2012 Dec 29.
Published in final edited form as: Science. 2012 May 11;336(6082):728–732. doi: 10.1126/science.1216338

Fig. 3. DNA-induced interdomain contacts are critical for DNA-dependent PARP-1 activation.

Fig. 3

(A) Surface representation of Zn1 and Zn3 bound to DNA. WGR and CAT have been omitted for clarity. (B) The Zn1 base-stacking loop, the Zn3 extended loop, and the 5'-terminated DNA strand form a binding site for WGR. (C) The Zn1–WGR–HD interface. (D) The HD-WGR–Zn3 interface. (E) The Zn3–Zn1 interface. Residues targeted for mutagenesis are labeled (yellow). Residues identified in a random screen for inactive mutants (20) are labeled (green). (F) SDS-PAGE assay of DNA-dependent PARP-1 automodification activity. WT and the indicated mutants were monitored for a shift in migration due to the covalent addition of PAR.