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A new DNA-binding motif in the Skn-1 binding domain–DNA complex

Nature Structural Biology volume 5, pages 484–491 (1998)Cite this article

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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Author notes

  1. Gary W. Daughdrill

    Present address: Department of Biology, University of Utah, Salt Lake City, Utah, 84112, USA

Authors and Affiliations

  1. Institute of Molecular Biology, University of Oregon, Eugene, Oregon, 97403, USA

    Peter B. Rupert, Gary W. Daughdrill, Bruce Bowerman & Brian W. Matthews

  2. Howard Hughes Medical Institute, University of Oregon, Eugene, Oregon, 97403, USA

    Peter B. Rupert & Brian W. Matthews

  3. Department of Biology, University of Oregon, Eugene, Oregon, 97403, USA

    Bruce Bowerman

  4. Department of Chemistry, University of Oregon, Eugene, Oregon, 97403, USA

    Peter B. Rupert & Gary W. Daughdrill

  5. Department of Physics, University of Oregon, Eugene, Oregon, 97403, USA

    Brian W. Matthews

Authors
  1. Peter B. Rupert
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  2. Gary W. Daughdrill
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  3. Bruce Bowerman
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  4. Brian W. Matthews
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Correspondence to Brian W. Matthews.

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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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