Authors: | Clark, K. L.; Halay, E. D.; Lai, E.; Burley, S. K. |
Article Title: | Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5 |
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 Å resolution. This α/β 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°bend. The transcription factor fold is very similar to the structure of histone H5. In its amino-terminal half, three α-helices adopt a compact structure that presents the third helix to the major groove. The remainder of the protein includes a twisted, antiparallel β-structure and random coil that interacts with the minor groove. © 1993 Nature Publishing Group. |
Keywords: | dna-binding proteins; protein conformation; animal; nuclear proteins; amino acid sequence; molecular sequence data; sequence homology, amino acid; molecular recognition; peptide fragments; base sequence; crystal structure; models, molecular; binding sites; rats; protein structure; x ray crystallography; histones; protein dna interaction; x-ray diffraction; priority journal; article; support, non-u.s. gov't; histone h5 |
Journal Title: | Nature |
Volume: | 364 |
Issue: | 6436 |
ISSN: | 0028-0836 |
Publisher: | Nature Publishing Group |
Date Published: | 1993-07-29 |
Start Page: | 412 |
End Page: | 420 |
Language: | English |
DOI: | 10.1038/364412a0 |
PUBMED: | 8332212 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Article -- Export Date: 1 March 2019 -- Source: Scopus |