Structural basis for the inhibition of poly(ADP-ribose) polymerases 1 and 2 by BMN 673, a potent inhibitor derived from dihydropyridophthalazinone

Aoyagi-Scharber, M.; Gardberg, A.S.; Yip, B.K.; Wang, B.; Shen, Y.; Fitzpatrick, P.A.

doi:10.1107/S2053230X14015088

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Binding mode of BMN 673. (a) Intricate network of hydrogen-bonding (dotted lines) and π-stacking interactions formed between BMN 673 and active-site residues (catPARP1–BMN 673 chain D and catPARP2–BMN 673 chain A). The novel disubstituted scaffold of BMN 673 leads to unique interactions with solvent molecules and extended pocket residues. (b) Binding interactions of BMN 673 at less conserved regions: the N-terminal helical domain (αF) and D-loop.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 70| Part 9| August 2014| Pages 1143-1149

doi:10.1107/S2053230X14015088

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