Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A

Science. 1991 May 10;252(5007):809-17. doi: 10.1126/science.2028256.


The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap part way around the double helix. Each finger has a similar relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha helix contact the bases, and most of the contracts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallography
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / isolation & purification
  • DNA-Binding Proteins / physiology
  • Early Growth Response Protein 1
  • Immediate-Early Proteins*
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Transcription Factors / chemistry*
  • Transcription Factors / isolation & purification
  • Transcription Factors / physiology
  • Zinc Fingers / physiology*


  • DNA-Binding Proteins
  • Early Growth Response Protein 1
  • Egr1 protein, mouse
  • Immediate-Early Proteins
  • Transcription Factors
  • DNA