1.
Angew Chem Int Ed Engl
; 50(29): 6511-5, 2011 Jul 11.
Article
in English
| MEDLINE
| ID: mdl-21656885
Subject(s)
Inteins , Protein Engineering , Protein Splicing , Amino Acid Sequence , DNA Polymerase III/chemistry , DNA Polymerase III/genetics , Kinetics , Molecular Sequence Data , Nostoc , Poly(ADP-ribose) Polymerases/biosynthesis , Poly(ADP-ribose) Polymerases/chemical synthesis , Static Electricity
2.
FEBS Lett
; 586(21): 3858-64, 2012 Nov 02.
Article
in English
| MEDLINE
| ID: mdl-23010590
ABSTRACT
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.