Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2012-06

AUTHORS

In-Kwon Kim, James R Kiefer, Chris M W Ho, Roderick A Stegeman, Scott Classen, John A Tainer, Tom Ellenberger

ABSTRACT

Reversible post-translational modification by poly(ADP-ribose) (PAR) regulates chromatin structure, DNA repair and cell fate in response to genotoxic stress. PAR glycohydrolase (PARG) removes PAR chains from poly ADP-ribosylated proteins to restore protein function and release oligo(ADP-ribose) chains to signal damage. Here we report crystal structures of mammalian PARG and its complex with a substrate mimic that reveal an open substrate-binding site and a unique 'tyrosine clasp' enabling endoglycosidic cleavage of branched PAR chains. More... »

PAGES

653

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.2305

DOI

http://dx.doi.org/10.1038/nsmb.2305

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012125629

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22609859


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