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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1997-3-20
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pubmed:abstractText |
The structure of a complex between the DNA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magnetic resonance spectroscopy. The GAGA-DBD comprises a single classical Cys2-His2 zinc finger core, and an N-terminal extension containing two highly basic regions, BR1 and BR2. The zinc finger core binds in the major groove and recognizes the first three GAG bases of the consensus in a manner similar to that seen in other classical zinc finger-DNA complexes. Unlike the latter, which require tandem zinc finger repeats with a minimum of two units for high affinity binding, the GAGA-DBD makes use of only a single finger complemented by BR1 and BR2. BR2 forms a helix that interacts in the major groove recognizing the last G of the consensus, while BR1 wraps around the DNA in the minor groove and recognizes the A in the fourth position of the consensus. The implications of the structure of the GAGA-DBD-DNA complex for chromatin remodelling are discussed.
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pubmed:commentsCorrections |
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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 |
Feb
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
122-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9033593-Amino Acid Sequence,
pubmed-meshheading:9033593-Base Sequence,
pubmed-meshheading:9033593-Binding Sites,
pubmed-meshheading:9033593-Consensus Sequence,
pubmed-meshheading:9033593-DNA,
pubmed-meshheading:9033593-DNA-Binding Proteins,
pubmed-meshheading:9033593-Drosophila Proteins,
pubmed-meshheading:9033593-Homeodomain Proteins,
pubmed-meshheading:9033593-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9033593-Models, Molecular,
pubmed-meshheading:9033593-Molecular Sequence Data,
pubmed-meshheading:9033593-Nucleic Acid Conformation,
pubmed-meshheading:9033593-Oligodeoxyribonucleotides,
pubmed-meshheading:9033593-Protein Conformation,
pubmed-meshheading:9033593-Protein Structure, Secondary,
pubmed-meshheading:9033593-Recombinant Proteins,
pubmed-meshheading:9033593-Transcription Factors
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pubmed:year |
1997
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pubmed:articleTitle |
The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode.
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pubmed:affiliation |
Laboratories of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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