2COM

The solution structure of the SWIRM domain of human LSD1

2COM の概要

• エントリーDOI: 10.2210/pdb2com/pdb
• NMR情報: BMRB: 10011
• 分子名称: Lysine-specific histone demethylase 1 (1 entity in total)
• 機能のキーワード: swirm domain, lsd1, aof2, kiaa0601, histone modulation, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: O60341
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13727.43

構造登録者

Tochio, N.,Umehara, T.,Koshiba, S.,Inoue, M.,Tanaka, A.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-05-18, 公開日: 2005-11-18, 最終更新日: 2024-05-29)

主引用文献

Tochio, N.,Umehara, T.,Koshiba, S.,Inoue, M.,Yabuki, T.,Aoki, M.,Seki, E.,Watanabe, S.,Tomo, Y.,Hanada, M.,Ikari, M.,Sato, M.,Terada, T.,Nagase, T.,Ohara, O.,Shirouzu, M.,Tanaka, A.,Kigawa, T.,Yokoyama, S.
Solution structure of the SWIRM domain of human histone demethylase LSD1
Structure, 14:457-468, 2006

PubMed Abstract: SWIRM is an evolutionarily conserved domain involved in several chromatin-modifying complexes. Recently, the LSD1 protein, which bears a SWIRM domain, was found to be a demethylase for Lys4-methylated histone H3. Here, we report a solution structure of the SWIRM domain of human LSD1. It forms a compact fold composed of 6 alpha helices, in which a 20 amino acid long helix (alpha4) is surrounded by 5 other short helices. The SWIRM domain structure could be divided into the N-terminal part (alpha1-alpha3) and the C-terminal part (alpha4-alpha6), which are connected to each other by a salt bridge. While the N-terminal part forms a SWIRM-specific structure, the C-terminal part adopts a helix-turn-helix (HTH)-related fold. We discuss a model in which the SWIRM domain acts as an anchor site for a histone tail.

PubMed: 16531230
DOI: 10.1016/j.str.2005.12.004

実験手法

SOLUTION NMR