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

Curr Top Microbiol Immunol. 2015;384:153-66. doi: 10.1007/82_2014_417.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ADP Ribose Transferases / chemistry*
  • ADP Ribose Transferases / genetics
  • ADP Ribose Transferases / metabolism
  • Amino Acid Sequence
  • Animals
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Multigene Family*
  • Sequence Alignment
  • Structural Homology, Protein

Substances

  • ADP Ribose Transferases