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Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5.
- Source :
-
Nature [Nature] 1993 Jul 29; Vol. 364 (6436), pp. 412-20. - Publication Year :
- 1993
-
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.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Hepatocyte Nuclear Factor 3-gamma
Models, Molecular
Molecular Sequence Data
Peptide Fragments chemistry
Protein Conformation
Rats
Sequence Homology, Amino Acid
X-Ray Diffraction
DNA-Binding Proteins chemistry
Histones chemistry
Nuclear Proteins chemistry
Transcription Factors
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 364
- Issue :
- 6436
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 8332212
- Full Text :
- https://doi.org/10.1038/364412a0