| Literature DB >> 23010590 |
Fahu He1, Kengo Tsuda, Mari Takahashi, Kanako Kuwasako, Takaho Terada, Mikako Shirouzu, Satoru Watanabe, Takanori Kigawa, Naohiro Kobayashi, Peter Güntert, Shigeyuki Yokoyama, Yutaka Muto.
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.Entities:
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Year: 2012 PMID: 23010590 DOI: 10.1016/j.febslet.2012.09.009
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124