Zinc-dependent structure of a single-finger domain of yeast ADR1

Science. 1988 Sep 16;241(4872):1489-92. doi: 10.1126/science.3047872.


In the proposed "zinc finger" DNA-binding motif, each repeat unit binds a zinc metal ion through invariant Cys and His residues and this drives the folding of each 30-residue unit into an independent nucleic acid-binding domain. To obtain structural information, we synthesized single and double zinc finger peptides from the yeast transcription activator ADR1, and assessed the metal-binding and DNA-binding properties of these peptides, as well as the solution structure of the metal-stabilized domains, with the use of a variety of spectroscopic techniques. A single zinc finger can exist as an independent structure sufficient for zinc-dependent DNA binding. An experimentally determined model of the single finger is proposed that is consistent with circular dichroism, one- and two-dimensional nuclear magnetic resonance, and visual spectroscopy of the single-finger peptide reconstituted in the presence of zinc.

MeSH terms

  • Circular Dichroism
  • DNA Mutational Analysis
  • DNA-Binding Proteins*
  • Magnetic Resonance Spectroscopy
  • Metalloproteins
  • Protein Conformation
  • Saccharomyces cerevisiae
  • Structure-Activity Relationship
  • Transcription Factors*
  • Zinc / physiology*


  • DNA-Binding Proteins
  • Metalloproteins
  • Transcription Factors
  • Zinc