Solution structure of the SWIRM domain of human histone demethylase LSD1

Naoya Tochio, Takashi Umehara, Seizo Koshiba, Makoto Inoue, Takashi Yabuki, Masaaki Aoki, Eiko Seki, Satoru Watanabe, Yasuko Tomo, Masaru Hanada, Masaomi Ikari, Miyuki Sato, Takaho Terada, Takahiro Nagase, Osamu Ohara, Mikako Shirouzu, Akiko Tanaka, Takanori Kigawa, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)


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 α helices, in which a 20 amino acid long helix (α4) is surrounded by 5 other short helices. The SWIRM domain structure could be divided into the N-terminal part (α1-α3) and the C-terminal part (α4-α6), 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.

Original languageEnglish
Pages (from-to)457-468
Number of pages12
Issue number3
Publication statusPublished - 2006 Mar


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