Abstract
The ADP-ribosylation of proteins is an important posttranslational 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.
Original language | English (US) |
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Pages (from-to) | 1911-1920 |
Number of pages | 10 |
Journal | EMBO Journal |
Volume | 24 |
Issue number | 11 |
DOIs | |
State | Published - Jun 1 2005 |
Externally published | Yes |
Keywords
- Ligand
- Metabolites
- NAD
- PARP
- Protein module
ASJC Scopus subject areas
- General Neuroscience
- Molecular Biology
- General Biochemistry, Genetics and Molecular Biology
- General Immunology and Microbiology