Abstract
GA-binding protein (GABP) is a transcriptional regulator composed of two structurally dissimilar subunits. The alpha subunit contains a DNA-binding domain that is a member of the ETS family, whereas the beta subunit contains a series of ankyrin repeats. The crystal structure of a ternary complex containing a GABPalpha/beta ETS domain-ankyrin repeat heterodimer bound to DNA was determined at 2. 15 angstrom resolution. The structure shows how an ETS domain protein can recruit a partner protein using both the ETS domain and a carboxyl-terminal extension and provides a view of an extensive protein-protein interface formed by a set of ankyrin repeats. The structure also reveals how the GABPalpha ETS domain binds to its core GGA DNA-recognition motif.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Ankyrins / chemistry
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Crystallography, X-Ray
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DNA / metabolism*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / metabolism*
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Dimerization
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GA-Binding Protein Transcription Factor
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Hydrogen Bonding
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation*
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Protein Structure, Secondary
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Proto-Oncogene Proteins / chemistry
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-ets
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Trans-Activators / chemistry
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Trans-Activators / metabolism
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Transcription Factors / chemistry*
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Transcription Factors / metabolism*
Substances
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Ankyrins
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DNA-Binding Proteins
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GA-Binding Protein Transcription Factor
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-ets
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Recombinant Proteins
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Trans-Activators
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Transcription Factors
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proto-oncogene protein Spi-1
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DNA