1PAX
THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH 3,4-DIHYDRO-5-METHYL-ISOQUINOLINONE
Summary for 1PAX
| Entry DOI | 10.2210/pdb1pax/pdb |
| Descriptor | POLY(ADP-RIBOSE) POLYMERASE, 3,4-DIHYDRO-5-METHYL-ISOQUINOLINONE (3 entities in total) |
| Functional Keywords | transferase, glycosyltransferase, nad(+) adp-ribosyltransferase |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Nucleus: P26446 |
| Total number of polymer chains | 1 |
| Total formula weight | 40576.55 |
| Authors | Ruf, A.,Schulz, G.E. (deposition date: 1996-05-06, release date: 1997-05-15, Last modification date: 2024-02-14) |
| Primary citation | Ruf, A.,Mennissier de Murcia, J.,de Murcia, G.,Schulz, G.E. Structure of the catalytic fragment of poly(ADP-ribose) polymerase from chicken. Proc.Natl.Acad.Sci.USA, 93:7481-7485, 1996 Cited by PubMed Abstract: The crystal structures of the catalytic fragment of chicken poly(ADP-ribose) polymerase [NAD+ ADP-ribosyltransferase; NAD+:poly(adenosine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyltransferase, EC 2.4.2.30] with and without a nicotinamide-analogue inhibitor have been elucidated. Because this enzyme is involved in the regulation of DNA repair, its inhibitors are of interest for cancer therapy. The inhibitor shows the nicotinamide site and also suggests the adenosine site. The enzyme is structurally related to bacterial ADP-ribosylating toxins but contains an additional alpha-helical domain that is suggested to relay the activation signal issued on binding to damaged DNA. PubMed: 8755499DOI: 10.1073/pnas.93.15.7481 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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