| Literature DB >> 19354255 |
Lari Lehtiö1, Ann-Sofie Jemth, Ruairi Collins, Olga Loseva, Andreas Johansson, Natalia Markova, Martin Hammarström, Alex Flores, Lovisa Holmberg-Schiavone, Johan Weigelt, Thomas Helleday, Herwig Schüler, Tobias Karlberg.
Abstract
Poly(ADP-ribose) polymerases (PARPs) activate DNA repair mechanisms upon stress- and cytotoxin-induced DNA damage, and inhibition of PARP activity is a lead in cancer drug therapy. We present a structural and functional analysis of the PARP domain of human PARP-3 in complex with several inhibitors. Of these, KU0058948 is the strongest inhibitor of PARP-3 activity. The presented crystal structures highlight key features for potent inhibitor binding and suggest routes for creating isoenzyme-specific PARP inhibitors.Entities:
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Year: 2009 PMID: 19354255 DOI: 10.1021/jm900052j
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446