1MD0

CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1

1MD0 の概要

• エントリーDOI: 10.2210/pdb1md0/pdb
• 関連するPDBエントリー: 1K79
• 分子名称: C-ets-1 protein (2 entities in total)
• 機能のキーワード: autoinhibition, transcription factor, transcription
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Nucleus: P27577
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32731.41

構造登録者

Garvie, C.W.,Pufall, M.A.,Graves, B.J.,Wolberger, C. (登録日: 2002-08-06, 公開日: 2002-12-11, 最終更新日: 2024-02-14)

主引用文献

Garvie, C.W.,Pufall, M.A.,Graves, B.J.,Wolberger, C.
Structural Analysis of the Autoinhibition of Ets-1 and Its Role in Protein Partnerships
J.Biol.Chem., 277:45529-45536, 2002

PubMed Abstract: The DNA-binding activity of the eukaryotic transcription factor Ets-1 (E26 avian erythroblastosis virus oncogene-E twenty-six) is negatively regulated by inhibitory regions that flank the ETS domain. Based on the results of solution studies, these N- and C-terminal inhibitory regions have been proposed to pack against the ETS domain and form an autoinhibitory module whose N terminus partially unfolds upon binding of Ets-1 to DNA. Mutations that disrupt autoinhibition of DNA binding also cause a structural change in the inhibitory region. We report here a crystallographic study of fragments of Ets-1 that provide structural details of the inhibitory module and the structural transition that accompanies DNA binding. The structures of free and DNA-bound Ets-1 fragments containing the ETS domain and the inhibitory regions confirm that the N-terminal inhibitory region contains two alpha-helices one of which unfolds upon Ets-1 binding to DNA. The observations from the crystal structure, coupled with mutagenesis experiments, allow us to propose a model for the inhibited form of Ets-1 and lend insight into the flexible interaction between Ets-1 and the acute myeloid leukemia 1 protein, AML1 (RUNX1).

PubMed: 12221090
DOI: 10.1074/jbc.M206327200

実験手法

X-RAY DIFFRACTION (2 Å)