1D9N
SOLUTION STRUCTURE OF THE METHYL-CPG-BINDING DOMAIN OF THE METHYLATION-DEPENDENT TRANSCRIPTIONAL REPRESSOR MBD1/PCM1
1D9N の概要
| エントリーDOI | 10.2210/pdb1d9n/pdb |
| 分子名称 | METHYL-CPG-BINDING PROTEIN MBD1 (1 entity in total) |
| 機能のキーワード | mbd, methyl-cpg, pcm1, methylation, dna binding domain, gene regulation |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 8516.75 |
| 構造登録者 | Ohki, I.,Shimotake, N.,Fujita, N.,Nakao, M.,Shirakawa, M. (登録日: 1999-10-28, 公開日: 2000-10-28, 最終更新日: 2024-05-22) |
| 主引用文献 | Ohki, I.,Shimotake, N.,Fujita, N.,Nakao, M.,Shirakawa, M. Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1. EMBO J., 18:6653-6661, 1999 Cited by PubMed Abstract: CpG methylation in vertebrates is important for gene silencing, alterations in chromatin structure and genomic stability, and differences in the DNA-methylation status are correlated with imprinting phenomena, carcinogenesis and embryonic development. Methylation signals are interpreted by protein factors that contain shared methyl-CpG-binding domains (MBDs). We have determined the solution structure of the MBD of the human methylation-dependent transcriptional repressor MBD1 by multi-dimensional heteronuclear NMR spectroscopy. It folds into an alpha/beta-sandwich structure with characteristic loops. Basic residues conserved in the MBD family are largely confined to one face of this fold and a flexible loop, which together form a large positively charged surface. Site-directed mutagenesis and chemical shift changes upon complexing with a methylated DNA facilitated identification of this surface as the DNA interaction site. In addition to three basic residues, conserved Tyr34 and Asp32 were shown to be important for the DNA binding. PubMed: 10581239DOI: 10.1093/emboj/18.23.6653 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
検証レポート(詳細版)
をダウンロード






