Comparative structural analysis of the putative mono-ADP-ribosyltransferases of the ARTD/PARP family.

Pinto AF, Schüler H

Curr. Top. Microbiol. Immunol. 384 (-) 153-166 [2014-07-13; online 2014-07-13]

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.

Protein Science Facility (PSF)

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PubMed 25015788

DOI 10.1007/82_2014_417

Crossref 10.1007/82_2014_417