1S5R

Solution Structure of HBP1 SID-mSin3A PAH2 Complex

1S5R の概要

• エントリーDOI: 10.2210/pdb1s5r/pdb
• 関連するPDBエントリー: 1S5Q
• NMR情報: BMRB: 4635
• 分子名称: high mobility group box transcription factor 1, Sin3a protein (2 entities in total)
• 機能のキーワード: protein-peptide complex, amphipathic helix motif, four-helix bundle, repressor-corepressor complex, transcription
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Nucleus: Q60520
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12922.34

構造登録者

Swanson, K.A.,Knoepfler, P.S.,Huang, K.,Kang, R.S.,Cowley, S.M.,Laherty, C.D.,Eisenman, R.N.,Radhakrishnan, I. (登録日: 2004-01-21, 公開日: 2004-07-06, 最終更新日: 2024-05-22)

主引用文献

Swanson, K.A.,Knoepfler, P.S.,Huang, K.,Kang, R.S.,Cowley, S.M.,Laherty, C.D.,Eisenman, R.N.,Radhakrishnan, I.
HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations.
Nat.Struct.Mol.Biol., 11:738-746, 2004

PubMed Abstract: Recruitment of the histone deacetylase (HDAC)-associated Sin3 corepressor is an obligatory step in many eukaryotic gene silencing pathways. Here we show that HBP1, a cell cycle inhibitor and regulator of differentiation, represses transcription in a HDAC/Sin3-dependent manner by targeting the mammalian Sin3A (mSin3A) PAH2 domain. HBP1 is unrelated to the Mad1 repressor for which high-resolution structures in complex with PAH2 have been described. We show that like Mad1, the HBP1 transrepression domain binds through a helical structure to the hydrophobic cleft of mSin3A PAH2. Notably, the HBP1 helix binds PAH2 in a reversed orientation relative to Mad1 and, equally unexpectedly, this is correlated with a chain reversal of the minimal Sin3 interaction motifs. These results not only provide insights into how multiple, unrelated transcription factors recruit the same coregulator, but also have implications for how sequence similarity searches are conducted.

PubMed: 15235594
DOI: 10.1038/nsmb798

実験手法

SOLUTION NMR