Structural insight into the interaction of ADP-ribose with the PARP WWE domains

FEBS Lett. 2012 Nov 2;586(21):3858-64. doi: 10.1016/j.febslet.2012.09.009. Epub 2012 Sep 22.


The WWE domain is often identified in proteins associated with ubiquitination or poly-ADP-ribosylation. Structural information about WWE domains has been obtained for the ubiquitination-related proteins, such as Deltex and RNF146, but not yet for the poly-ADP-ribose polymerases (PARPs). Here we determined the solution structures of the WWE domains from PARP11 and PARP14, and compared them with that of the RNF146 WWE domain. NMR perturbation experiments revealed the specific differences in their ADP-ribose recognition modes that correlated with their individual biological activities. The present structural information sheds light on the ADP-ribose recognition modes by the PARP WWE domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / chemistry*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Computer Simulation
  • Humans
  • Magnetic Resonance Spectroscopy
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Poly(ADP-ribose) Polymerases / chemical synthesis*
  • Poly(ADP-ribose) Polymerases / chemistry
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Ubiquitin-Protein Ligases / chemical synthesis*
  • Ubiquitin-Protein Ligases / chemistry


  • Adenosine Diphosphate Ribose
  • Ubiquitin-Protein Ligases
  • Parp14 protein, mouse
  • Poly(ADP-ribose) Polymerases
  • poly(ADP-ribose) polymerase-11, mouse