4F0D

Human ARTD15/PARP16 IN COMPLEX WITH 3-AMINOBENZAMIDE

Summary for 4F0D

• Entry DOI: 10.2210/pdb4f0d/pdb
• Descriptor: Poly [ADP-ribose] polymerase 16, 3-aminobenzamide (2 entities in total)
• Functional Keywords: transferase, adp-ribose, parp16, artd15, structural genomics, structural genomics consortium, sgc, artd transferase domain, adp-ribosylation, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass membrane protein (Potential): Q8N5Y8
• Total number of polymer chains: 2
• Total formula weight: 62357.31

Authors

Karlberg, T.,Thorsell, A.G.,Kallas, A.,Schuler, H.,Structural Genomics Consortium (SGC) (deposition date: 2012-05-04, release date: 2012-06-13, Last modification date: 2024-02-28)

Primary citation

Karlberg, T.,Thorsell, A.G.,Kallas, A.,Schuler, H.
Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory Domain.
J.Biol.Chem., 287:24077-24081, 2012

PubMed Abstract: ADP-ribosylation is involved in the regulation of DNA repair, transcription, and other processes. The 18 human ADP-ribose transferases with diphtheria toxin homology include ARTD1/PARP1, a cancer drug target. Knowledge of other family members may guide therapeutics development and help evaluate potential drug side effects. Here, we present the crystal structure of human ARTD15/PARP16, a previously uncharacterized enzyme. ARTD15 features an α-helical domain that packs against its transferase domain without making direct contact with the NAD(+)-binding crevice or the donor loop. Thus, this novel domain does not resemble the regulatory domain of ARTD1. ARTD15 displays auto-mono(ADP-ribosylation) activity and is affected by canonical poly(ADP-ribose) polymerase inhibitors. These results add to a framework that will facilitate research on a medically important family of enzymes.

PubMed: 22661712
DOI: 10.1074/jbc.M112.379289

Experimental method

X-RAY DIFFRACTION (2.7 Å)