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


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
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  1. Eseng Lai
    45 Lai