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The macro domain is an ADP‐ribose binding module

The macro domain is an ADP‐ribose binding module The ADP‐ribosylation of proteins is an important post‐translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long‐term memory formation. Yet no protein modules are known that specifically recognize the ADP‐ribose nucleotide. We provide biochemical and structural evidence that macro domains are high‐affinity ADP‐ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP‐ribose. In addition, some macro domain proteins also recognize poly‐ADP‐ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP‐ribose. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

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References (80)

Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1038/sj.emboj.7600664
pmid
15902274
Publisher site
See Article on Publisher Site

Abstract

The ADP‐ribosylation of proteins is an important post‐translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long‐term memory formation. Yet no protein modules are known that specifically recognize the ADP‐ribose nucleotide. We provide biochemical and structural evidence that macro domains are high‐affinity ADP‐ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP‐ribose. In addition, some macro domain proteins also recognize poly‐ADP‐ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP‐ribose.

Journal

The EMBO JournalWiley

Published: Jan 1, 2005

Keywords: ; ; ; ;

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