Tochio Naoya, Umehara Takashi, Koshiba Seizo, Inoue Makoto, Yabuki Takashi, Aoki Masaaki, Seki Eiko, Watanabe Satoru, Tomo Yasuko, Hanada Masaru, Ikari Masaomi, Sato Miyuki, Terada Takaho, Nagase Takahiro, Ohara Osamu, Shirouzu Mikako, Tanaka Akiko, Kigawa Takanori, Yokoyama Shigeyuki
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Structure. 2006 Mar;14(3):457-68. doi: 10.1016/j.str.2005.12.004.
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.
SWIRM是一种参与多种染色质修饰复合物的进化保守结构域。最近，带有SWIRM结构域的LSD1蛋白被发现是赖氨酸4甲基化组蛋白H3的去甲基化酶。在此，我们报道了人LSD1的SWIRM结构域的溶液结构。它形成了一个由6个α螺旋组成的紧密折叠结构，其中一个20个氨基酸长的螺旋（α4）被其他5个短螺旋包围。SWIRM结构域结构可分为N端部分（α1-α3）和C端部分（α4-α6），它们通过一个盐桥相互连接。虽然N端部分形成了SWIRM特异性结构，但C端部分采用了一种与螺旋-转角-螺旋（HTH）相关的折叠结构。我们讨论了一个模型，其中SWIRM结构域作为组蛋白尾巴 的锚定位点。
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