2O49
Crystal Structure of the N-terminal CUT domain of SATB1 Bound to Matrix Attachment Region DNA
2O49 の概要
エントリーDOI | 10.2210/pdb2o49/pdb |
関連するPDBエントリー | 1YSE 2O4A |
分子名称 | DNA (5'-D(*DGP*DCP*DTP*DAP*DAP*DTP*DAP*DTP*DAP*DTP*DGP*DC)-3'), DNA (5'-D(*DGP*DCP*DAP*DTP*DAP*DTP*DAP*DTP*DTP*DAP*DGP*DC)-3'), DNA-binding protein SATB1, ... (4 entities in total) |
機能のキーワード | protein-dna complex, transcription, transcription-dna complex, transcription/dna |
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 | 3 |
化学式量合計 | 18275.21 |
構造登録者 | |
主引用文献 | Yamasaki, K.,Akiba, T.,Yamasaki, T.,Harata, K. Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB1. Nucleic Acids Res., 35:5073-5084, 2007 Cited by PubMed Abstract: Special AT-rich sequence binding protein 1 (SATB1) regulates gene expression essential in immune T-cell maturation and switching of fetal globin species, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin remodeling. Previously we have revealed a five-helix structure of the N-terminal CUT domain, which is essentially the folded region in the MAR-binding domain, of human SATB1 by NMR. Here we determined crystal structure of the complex of the CUT domain and a MAR DNA, in which the third helix of the CUT domain deeply enters the major groove of DNA in the B-form. Bases of 5'-CTAATA-3' sequence are contacted by this helix, through direct and water-mediated hydrogen bonds and apolar and van der Waals contacts. Mutations at conserved base-contacting residues, Gln402 and Gly403, reduced the DNA-binding activity, which confirmed the importance of the observed interactions involving these residues. A significant number of equivalent contacts are observed also for typically four-helix POU-specific domains of POU-homologous proteins, indicating that these domains share a common framework of the DNA-binding mode, recognizing partially similar DNA sequences. PubMed: 17652321DOI: 10.1093/nar/gkm504 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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