Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5

Nature. 1993 Jul 29;364(6436):412-20. doi: 10.1038/364412a0.


The three-dimensional structure of an HNF-3/fork head DNA-recognition motif complexed with DNA has been determined by X-ray crystallography at 2.5 A resolution. This alpha/beta protein binds B-DNA as a monomer, through interactions with the DNA backbone and through both direct and water-mediated major and minor groove base contacts, inducing a 13 degrees bend. The transcription factor fold is very similar to the structure of histone H5. In its amino-terminal half, three alpha-helices adopt a compact structure that presents the third helix to the major groove. The remainder of the protein includes a twisted, antiparallel beta-structure and random coil that interacts with the minor groove.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • DNA-Binding Proteins / chemistry*
  • Hepatocyte Nuclear Factor 3-gamma
  • Histones / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry*
  • Peptide Fragments / chemistry
  • Protein Conformation
  • Rats
  • Sequence Homology, Amino Acid
  • Transcription Factors*
  • X-Ray Diffraction


  • DNA-Binding Proteins
  • Foxa3 protein, rat
  • Histones
  • Nuclear Proteins
  • Peptide Fragments
  • Transcription Factors
  • Hepatocyte Nuclear Factor 3-gamma