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- Title
The macro domain is an ADP-ribose binding module.
- Authors
Karras, Georgios I; Kustatscher, Georg; Buhecha, Heeran R; Allen, Mark D; Pugieux, Céline; Sait, Fiona; Bycroft, Mark; Ladurner, Andreas G
- 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.
- Publication
The EMBO journal, 2005, Vol 24, Issue 11, p1911
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1038/sj.emboj.7600664