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DNA-binding properties and secondary structural model of the hepatocyte nuclear factor 3/fork head domain. Export

Proceedings of the National Academy of Sciences USA, Vol. 90 (1993), pp. 11583-11587.

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amino_acid_sequence article base_sequence binding_sites caenorhabditis_elegans caenorhabditis_elegans_metabolism celegans c_elegans cloning_molecular consensus_sequence conserved_sequence dna_binding_proteins_chemistry dna_binding_proteins_metabolism drosophila_metabolism elegans mice molecular_sequence_data nematode nuclear_proteins_chemistry nuclear_proteins_metabolism oligodeoxyribonucleotides_chemical_synthesis oligodeoxyribonucleotides_metabolism polymerase_chain_reaction protein_structure_secondary rats recombinant_fusion_proteins_biosynthesis recombinant_proteins_chemistry recombinant_proteins_metabolism saccharomyces_cerevisiae_metabolism sequence_homology_amino_acid transcription_factors_chemistry transcription_factors_metabolism wormbase xenopus

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An 84-amino acid segment of QRF-1 [glutamine (Q)-rich factor 1], a newly cloned, B-cell-derived DNA-binding protein, shows significant sequence homology with the DNA-binding domains of the hepatocyte nuclear factor 3/fork head family of proteins. Here we demonstrate that this 84-amino acid domain is necessary and sufficient for DNA binding. We also propose a secondary structural model for the domain. At the N-terminal portion of the model, a basic hook structure is followed by two amphipathic helices separated by a turn. Invariant amino acid residues within the two proposed helices form the hydrophobic cores. An aromatic kink and a third amphipathic helix comprise the center of the domain. At the C terminus, two variable-length loops flank a putative 7-amino acid helix followed by a short basic region.


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