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Vol. 14, No. 14, pp. 1750-1764, July 15, 2000
1 Center for Molecular Oncology, Departments of
Biochemistry & Molecular Biology and Chemistry, The University of
Chicago, Chicago, Illinois 60637-5419 USA; 2 Gryphon Sciences,
South San Francisco, California 94080 USA; 3 Department of
Biochemistry, Case Western Reserve School of Medicine, Cleveland, Ohio
44106-4935 USA
Sex determination is regulated by diverse pathways. Although
upstream signals vary, a cysteine-rich DNA-binding domain (the DM
motif) is conserved within downstream transcription factors of
Drosophila melanogaster (Doublesex) and Caenorhabditis
elegans (MAB-3). Vertebrate DM genes have likewise been identified
and, remarkably, are associated with human sex reversal (46, XY gonadal dysgenesis). Here we demonstrate that the structure of the Doublesex domain contains a novel zinc module and disordered tail. The module consists of intertwined CCHC and HCCC Zn2+-binding sites; the
tail functions as a nascent recognition 
-helix. Mutations in either
Zn2+-binding site or tail can lead to an intersex phenotype.
The motif binds in the DNA minor groove without sharp DNA bending.
These molecular features, unusual among zinc fingers and zinc modules, underlie the organization of a Drosophila enhancer that
integrates sex- and tissue-specific signals. The structure provides a
foundation for analysis of DM mutations affecting sexual dimorphism and
courtship behavior.
[Key Words: Drosophila melanogaster; DNA-binding protein; gene regulation; transcription factor; NMR]
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