Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5.
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.
Clark
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Laboratory of Molecular Biophysics, Rockefeller University, New York, New York 10021.
Halay
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Lai
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Burley
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry*; D051543:Hepatocyte Nuclear Factor 3-gamma; D006657:Histones / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors; D014961:X-Ray Diffraction
D004268:DNA-Binding Proteins; C496507:Foxa3 protein, rat; D006657:Histones; D009687:Nuclear Proteins; D010446:Peptide Fragments; D014157:Transcription Factors; D051543:Hepatocyte Nuclear Factor 3-gamma