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1LPV

DROSOPHILA MELANOGASTER DOUBLESEX (DSX), NMR, 18 STRUCTURES

1LPV の概要
エントリーDOI10.2210/pdb1lpv/pdb
分子名称Doublesex protein, ZINC ION (2 entities in total)
機能のキーワードtranscription, drosophila melanogaster, dna binding, gene regulation
細胞内の位置Nucleus: P23023
タンパク質・核酸の鎖数1
化学式量合計6256.15
構造登録者
Zhu, L.,Wilken, J.,Phillips, N.,Narendra, U.,Chan, G.,Stratton, S.,Kent, S.,Weiss, M.A. (登録日: 2002-05-08, 公開日: 2002-10-02, 最終更新日: 2024-05-22)
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1lpv
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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