Abstract
Members of the ets family of transcription factors share a conserved DNA-binding domain, the ets domain. By using multidimensional NMR, we have determined the structure of the ets domain of human Fli-1 in the DNA-bound form. It consists of three alpha-helices and a four-stranded beta-sheet, similar to structures of the class of helix-turn-helix DNA binding proteins first found in the catabolite activator protein of Escherichia coli. NMR and mutagenesis experiments suggest that in comparison to structurally related proteins, the ets domain uses a new variation of the helix-turn-helix motif for binding to DNA.
MeSH terms
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Amino Acid Sequence
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DNA / metabolism
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Helix-Loop-Helix Motifs / genetics
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Helix-Loop-Helix Motifs / physiology
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Humans
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In Vitro Techniques
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Sequence Data
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Molecular Structure
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Mutagenesis, Site-Directed
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Protein Structure, Secondary
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Proto-Oncogene Protein c-fli-1
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Proto-Oncogene Proteins / chemistry
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-ets
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Solutions
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Trans-Activators / chemistry*
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Trans-Activators / genetics
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Trans-Activators / metabolism
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Transcription Factors*
Substances
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DNA-Binding Proteins
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Proto-Oncogene Protein c-fli-1
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-ets
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Solutions
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Trans-Activators
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Transcription Factors
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DNA