1LPV

DROSOPHILA MELANOGASTER DOUBLESEX (DSX), NMR, 18 STRUCTURES

Summary for 1LPV

• Entry DOI: 10.2210/pdb1lpv/pdb
• Descriptor: Doublesex protein, ZINC ION (2 entities in total)
• Functional Keywords: transcription, drosophila melanogaster, dna binding, gene regulation
• Cellular location: Nucleus: P23023
• Total number of polymer chains: 1
• Total formula weight: 6256.15

Authors

Zhu, L.,Wilken, J.,Phillips, N.,Narendra, U.,Chan, G.,Stratton, S.,Kent, S.,Weiss, M.A. (deposition date: 2002-05-08, release date: 2002-10-02, Last modification date: 2024-05-22)

Primary citation

Zhu, L.,Wilken, J.,Phillips, N.B.,Narendra, U.,Chan, G.,Stratton, S.M.,Kent, S.B.,Weiss, M.A.
Sexual dimorphism in diverse metazoans is regulated by a novel class of intertwined zinc fingers.
Genes Dev., 14:1750-1764, 2000

PubMed Abstract: 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 Zn(2+)-binding sites; the tail functions as a nascent recognition alpha-helix. Mutations in either Zn(2+)-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.

PubMed: 10898790
DOI: 10.1101/gad.189500

Experimental method

SOLUTION NMR