Abstract
The 500 MHz 1H NMR spectrum of a 68-residue peptide, encompassing the rat thyroid transcription factor 1 homeodomain (TTF-1 HD), was fully assigned using standard 2D NMR methodology. The secondary structure elements and their spatial organization were determined and led to a structure very similar to that previously described for other homeodomains and expected also for TTF-1 HD from homology modeling predictions. The three-dimensional arrangement of the three helix fragments of TTF-1 HD preserves the helix-turn-helix motif commonly occurring in many classes of DNA-binding proteins.
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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Animals
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DNA-Binding Proteins / chemistry*
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Magnetic Resonance Spectroscopy / methods
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Molecular Sequence Data
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Nuclear Proteins / biosynthesis
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Nuclear Proteins / chemistry*
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Protein Structure, Secondary*
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Rats
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Thyroid Nuclear Factor 1
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Transcription Factors / biosynthesis
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Transcription Factors / chemistry*
Substances
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DNA-Binding Proteins
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Nkx2-1 protein, rat
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Nuclear Proteins
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Recombinant Proteins
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Thyroid Nuclear Factor 1
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Transcription Factors