Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor

J Mol Biol. 2000 Dec 15;304(5):723-9. doi: 10.1006/jmbi.2000.4308.


The PHD (plant homeo domain) is a approximately 50-residue motif found mainly in proteins involved in eukaryotic transcription regulation. The characteristic sequence feature is a conserved Cys(4)-HisCys(3) zinc binding motif. We have determined the solution structure of the PHD motif from the human Williams-Beuren syndrome transcription factor (WSTF) protein. The domain folds into an interleaved zinc finger which binds two Zn(2+) in a similar manner to that of the RING and FYVE domains. The structure reveals a conserved zinc-binding core, together with two variable loops that are likely candidates for interactions between the various PHD domains and their specific ligands.

MeSH terms

  • Amino Acid Sequence
  • Homeodomain Proteins / chemistry*
  • Homeodomain Proteins / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism
  • Williams Syndrome*
  • Zinc / metabolism
  • Zinc Fingers / physiology*


  • Homeodomain Proteins
  • Peptide Fragments
  • Transcription Factors
  • Zinc

Associated data

  • PDB/1F62
  • SWISSPROT/Q92793