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

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

K L Clark  1 , E D Halay, E Lai, S K Burley
Affiliations

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

K L Clark et al. Nature. .

Abstract

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.

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