Abstract
The DNA-binding domain of Skn-1, a developmental transcription factor that specifies mesoderm in C. elegans, is shown by X-ray crystallography to have a novel fold in which a compact, monomeric, four-helix unit organizes two DNA-contact elements. At the C-terminus, a helix extends from the domain to occupy the major groove of DNA in a manner similar to bZip proteins. Skn-1, however, lacks the leucine zipper found in all bZips. Additional contacts with the DNA are made by a short basic segment at the N-terminus of the domain, reminiscent of the 'homeodomain arm'.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Composition
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Caenorhabditis elegans / chemistry*
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Caenorhabditis elegans / embryology
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Caenorhabditis elegans Proteins*
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Conserved Sequence
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Crystallography, X-Ray
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DNA / chemistry
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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Dimerization
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Fungal Proteins / chemistry
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Helminth Proteins / chemistry*
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Helminth Proteins / genetics
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Homeodomain Proteins / chemistry
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Nucleic Acid Conformation
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Protein Folding
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Protein Kinases / chemistry
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Protein Structure, Tertiary
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Transcription Factors / chemistry
Substances
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Caenorhabditis elegans Proteins
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DNA-Binding Proteins
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Fungal Proteins
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Helminth Proteins
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Homeodomain Proteins
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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skn-1 protein, C elegans
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DNA
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Protein Kinases