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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6436
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pubmed:dateCreated |
1993-8-16
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
364
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
412-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8332212-Amino Acid Sequence,
pubmed-meshheading:8332212-Animals,
pubmed-meshheading:8332212-Base Sequence,
pubmed-meshheading:8332212-Binding Sites,
pubmed-meshheading:8332212-DNA-Binding Proteins,
pubmed-meshheading:8332212-Hepatocyte Nuclear Factor 3-gamma,
pubmed-meshheading:8332212-Histones,
pubmed-meshheading:8332212-Models, Molecular,
pubmed-meshheading:8332212-Molecular Sequence Data,
pubmed-meshheading:8332212-Nuclear Proteins,
pubmed-meshheading:8332212-Peptide Fragments,
pubmed-meshheading:8332212-Protein Conformation,
pubmed-meshheading:8332212-Rats,
pubmed-meshheading:8332212-Sequence Homology, Amino Acid,
pubmed-meshheading:8332212-Transcription Factors,
pubmed-meshheading:8332212-X-Ray Diffraction
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pubmed:year |
1993
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pubmed:articleTitle |
Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5.
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pubmed:affiliation |
Laboratory of Molecular Biophysics, Rockefeller University, New York, New York 10021.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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