3c4h
Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor DR2313Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor DR2313
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPoly(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. Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3.,Lehtio L, Jemth AS, Collins R, Loseva O, Johansson A, Markova N, Hammarstrom M, Flores A, Holmberg-Schiavone L, Weigelt J, Helleday T, Schuler H, Karlberg T J Med Chem. 2009 May 14;52(9):3108-11. PMID:19354255[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- Homo sapiens
- Arrowsmith, C H.
- Berg, S Van den.
- Berglund, H.
- Bountra, C.
- Busam, R.
- Collins, R.
- Dahlgren, L G.
- Edwards, A M.
- Flodin, S.
- Flores, A.
- Graslund, S.
- Hammarstrom, M.
- Herman, M D.
- Johansson, A.
- Johansson, I.
- Kallas, A.
- Karlberg, T.
- Kotenyova, T.
- Lehtio, L.
- Moche, M.
- Nilsson, M E.
- Nordlund, P.
- Nyman, T.
- Persson, C.
- SGC, Structural Genomics Consortium.
- Sagemark, J.
- Svensson, L.
- Thorsell, A G.
- Tresaugues, L.
- Weigelt, J.
- Welin, M.
- Catalytic fragment
- Enzyme-inhibitor complex
- Glycosyltransferase
- Nad
- Nucleus
- Sgc
- Structural genomic
- Structural genomics consortium
- Transferase