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1ZV1

Crystal structure of the dimerization domain of doublesex protein from D. melanogaster

1ZV1 の概要
エントリーDOI10.2210/pdb1zv1/pdb
分子名称Doublesex protein (2 entities in total)
機能のキーワードdoublesex, uba domain, dimerization, sex determination, transcription factor, protein binding
由来する生物種Drosophila melanogaster (fruit fly)
タンパク質・核酸の鎖数2
化学式量合計15491.47
構造登録者
Weiss, M.A.,Bayrer, J.R.,Wan, Z.,Li, B.,Phillips, N.B. (登録日: 2005-06-01, 公開日: 2005-08-09, 最終更新日: 2024-02-14)
主引用文献Bayrer, J.R.,Zhang, W.,Weiss, M.A.
Dimerization of doublesex is mediated by a cryptic ubiquitin-associated domain fold: implications for sex-specific gene regulation
J.Biol.Chem., 280:32989-32996, 2005
Cited by
PubMed Abstract: Male- and female-specific isoforms of the Doublesex (DSX) transcription factor regulate somatic sexual differentiation in Drosophila. The isoforms (DSX(M) and DSX(F)) share an N-terminal DNA binding domain (the DM motif), broadly conserved among metazoan sex-determining pathways. DM-DNA recognition is enhanced by a C-terminal dimerization domain. The crystal structure of this domain, determined at a resolution of 1.6 A, reveals a novel dimeric arrangement of ubiquitin-associated (UBA) folds. Although this alpha-helical motif is well characterized in pathways of DNA repair and subcellular trafficking, to our knowledge this is its first report in a transcription factor. Dimerization is mediated by a non-canonical hydrophobic interface extrinsic to the putative ubiquitin binding surface. Key side chains at this interface, identified by alanine scanning mutagenesis, are conserved among DSX homologs. The mechanism of dimerization is thus unrelated to the low affinity domain swapping observed among ubiquitin-associated CUE domains. The unexpected observation of a ubiquitin-associated fold in DSX extends the repertoire of alpha-helical dimerization elements in transcription factors. The possibility that the ubiquitination machinery participates in the regulation of sexual dimorphism is discussed.
PubMed: 16049008
DOI: 10.1074/jbc.M507990200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 1zv1
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2024-10-30に公開中

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