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Structural insight into the interaction of ADP-ribose with the PARP WWE domains.
He, Fahu; Tsuda, Kengo; Takahashi, Mari; Kuwasako, Kanako; Terada, Takaho; Shirouzu, Mikako; Watanabe, Satoru; Kigawa, Takanori; Kobayashi, Naohiro; Güntert, Peter; Yokoyama, Shigeyuki; Muto, Yutaka.
Affiliation
  • He F; RIKEN Systems and Structural Biology Center, Tsurumi-ku, Yokohama, Kanagawa, Japan.
FEBS Lett ; 586(21): 3858-64, 2012 Nov 02.
Article in En | 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.
Subject(s)

Full text: 1 Database: MEDLINE Main subject: Adenosine Diphosphate Ribose / Poly(ADP-ribose) Polymerases / Ubiquitin-Protein Ligases Limits: Animals / Humans Language: En Year: 2012 Type: Article

Full text: 1 Database: MEDLINE Main subject: Adenosine Diphosphate Ribose / Poly(ADP-ribose) Polymerases / Ubiquitin-Protein Ligases Limits: Animals / Humans Language: En Year: 2012 Type: Article