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’.
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Rupert, P., Daughdrill, G., Bowerman, B. et al. A new DNA-binding motif in the Skn-1 binding domain–DNA complex. Nat Struct Mol Biol 5, 484–491 (1998). https://doi.org/10.1038/nsb0698-484
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DOI: https://doi.org/10.1038/nsb0698-484
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