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Updated: Jun 18, 2026

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The macro domain is an ADP-ribose binding module.

Georgios I Karras1, Georg Kustatscher, Heeran R Buhecha

  • 1Gene Expression Programme and Structural & Computational Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.

The EMBO Journal
|May 20, 2005
PubMed
Summary
This summary is machine-generated.

Macro domains are identified as high-affinity binding modules for ADP-ribose, a crucial molecule in biological processes. This discovery sheds light on the function of macro domain proteins in ADP-ribose biology.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • ADP-ribosylation is a vital post-translational modification involved in DNA repair, transcription, and memory formation.
  • Specific protein modules for recognizing ADP-ribose have remained elusive.

Purpose of the Study:

  • To identify protein modules that specifically bind ADP-ribose.
  • To elucidate the structural basis of ADP-ribose recognition by these modules.

Main Methods:

  • Biochemical assays to assess binding affinity.
  • X-ray crystallography to determine protein-ligand complex structures.
  • Analysis of conserved structural features within macro domains.

Main Results:

  • Macro domains exhibit high-affinity binding to ADP-ribose.
  • A conserved ligand-binding pocket was identified within the macro domain fold.
  • Human macro domains demonstrated conserved ADP-ribose binding capabilities.
  • Some macro domains were also found to bind poly-ADP-ribose.

Conclusions:

  • Macro domains function as specific ADP-ribose binding modules.
  • The conserved structure of macro domains facilitates ADP-ribose recognition.
  • Proteins containing macro domains play a significant role in ADP-ribose-related biological processes.