| Literature DB >> 16531230 |
Naoya Tochio1, 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.
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.Entities:
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Year: 2006 PMID： 16531230 DOI： 10.1016/j.str.2005.12.004
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006