Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
Copyright policy )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.
- Rockefeller University United States
- Howard Hughes Medical Institute United States
- Memorial Sloan Kettering Cancer Center United States
Models, Molecular, Binding Sites, Base Sequence, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Nuclear Proteins, Peptide Fragments, Rats, DNA-Binding Proteins, Histones, X-Ray Diffraction, Animals, Amino Acid Sequence, Hepatocyte Nuclear Factor 3-gamma, Transcription Factors
Models, Molecular, Binding Sites, Base Sequence, Sequence Homology, Amino Acid, Protein Conformation, Molecular Sequence Data, Nuclear Proteins, Peptide Fragments, Rats, DNA-Binding Proteins, Histones, X-Ray Diffraction, Animals, Amino Acid Sequence, Hepatocyte Nuclear Factor 3-gamma, Transcription Factors
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