Comparative Structural Analysis of the Putative Mono-ADP-Ribosyltransferases of the ARTD/PARP Family
The existence and significance of endogenous cytosolic and nuclear mono-ADP-ribosylation has been a matter of debate. Today, evidence suggests that the human enzymes that catalyze the reaction have been rounded up. Moreover, substrate proteins and specific functions for mono-ADP-ribosyltransferases are beginning to be defined. Reader domains that specifically recognize mono-ADP-ribosylated target proteins and erasers that remove the mono-ADP-ribosyl mark have been identified. Here, we review the contribution of crystal structures to our understanding of the putative mono-ADP-ribosyltransferases with Diphtheria toxin and ARTD1/PARP1 homology.
KeywordsPARP Inhibitor Diphtheria Toxin Bacterial Toxin Transferase Domain Nicotinamide Moiety
ADP-ribosyltransferases with Clostridium toxin homology
ADP-ribosyltransferases with Diphtheria toxin homology
Mono-ADP-ribosylating ARTD enzymes
The majority of available mARTD crystal structures have been solved through funding by the Structural Genomics Consortium (www.thesgc.org). We wish to thank Torun Ekblad, Tobias Karlberg, Mirjam Klepsch, Ann-Gerd Thorsell, Patricia Verheugd, and Johan Weigelt for discussions, as well as Martin Moche (Protein Science Facility at Karolinska Institutet) and members of the Structural Genomics Consortium for their roles in solving mARTD crystal structures. Work in the laboratory is funded by the Swedish Foundation for Strategic Research, the Swedish Research Council, the Swedish Cancer Society, and the IngaBritt och Arne Lundbergs Research Foundation.
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