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1YSE

Solution structure of the MAR-binding domain of SATB1

1YSE の概要
エントリーDOI10.2210/pdb1yse/pdb
分子名称DNA-binding protein SATB1 (1 entity in total)
機能のキーワードall helical, dna-binding domain, t-cell development, dna binding protein
由来する生物種Homo sapiens (human)
細胞内の位置Nucleus matrix: Q01826
タンパク質・核酸の鎖数1
化学式量合計15807.69
構造登録者
Yamasaki, K.,Yamaguchi, H. (登録日: 2005-02-08, 公開日: 2006-01-03, 最終更新日: 2024-05-29)
主引用文献Yamaguchi, H.,Tateno, M.,Yamasaki, K.
Solution Structure and DNA-binding Mode of the Matrix Attachment Region-binding Domain of the Transcription Factor SATB1 That Regulates the T-cell Maturation
J.Biol.Chem., 281:5319-5327, 2006
Cited by
PubMed Abstract: SATB1 is a transcriptional regulator controlling the gene expression that is essential in the maturation of the immune T-cell. SATB1 binds to the nuclear matrix attachment regions of DNA, where it recruits histone deacetylase and represses transcription through a local chromatin remodeling. Here we determined the solution structure of the matrix attachment region-binding domain, possessing similarity to the CUT DNA-binding domain, of human SATB1 by NMR spectroscopy. The structure consists of five alpha-helices, in which the N-terminal four are arranged similarly to the four-helix structure of the CUT domain of hepatocyte nuclear factor 6alpha. By an NMR chemical shift perturbation analysis and by surface plasmon resonance analyses of SATB1 mutant proteins, an interface for DNA binding was revealed to be located at the third helix and the surrounding regions. Surface plasmon resonance experiments using groove-specific binding drugs and methylated DNAs indicated that the domain recognizes DNA from the major groove side. These observations suggested that SATB1 possesses a DNA-binding mode similar to that of the POU-specific DNA-binding domain, which is known to share structural similarity to the four-helix CUT domain.
PubMed: 16371359
DOI: 10.1074/jbc.M510933200
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 1yse
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2026-04-22に公開中

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