2DCE

Solution structure of the SWIRM domain of human KIAA1915 protein

2DCE の概要

• エントリーDOI: 10.2210/pdb2dce/pdb
• 分子名称: KIAA1915 protein (1 entity in total)
• 機能のキーワード: swirm domain, kiaa1915, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, unknown function
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q5VVJ2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12829.41

構造登録者

Yoneyama, M.,Tochio, N.,Umehara, T.,Koshiba, S.,Inoue, M.,Tanaka, A.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2006-01-06, 公開日: 2006-07-06, 最終更新日: 2024-05-29)

主引用文献

Yoneyama, M.,Tochio, N.,Umehara, T.,Koshiba, S.,Inoue, M.,Yabuki, T.,Aoki, M.,Seki, E.,Matsuda, T.,Watanabe, S.,Tomo, Y.,Nishimura, Y.,Harada, T.,Terada, T.,Shirouzu, M.,Hayashizaki, Y.,Ohara, O.,Tanaka, A.,Kigawa, T.,Yokoyama, S.
Structural and Functional Differences of SWIRM Domain Subtypes
J.Mol.Biol., 369:222-238, 2007

PubMed Abstract: SWIRM is a conserved domain found in several chromatin-associated proteins. Based on their sequences, the SWIRM family members can be classified into three subfamilies, which are represented by Swi3, LSD1, and Ada2. Here we report the SWIRM structure of human MYb-like, Swirm and Mpn domain-containing protein-1 (MYSM1). The MYSM1 SWIRM structure forms a compact HTH-related fold comprising five alpha-helices, which best resembles the Swi3 SWIRM structure, among the known SWIRM structures. The MYSM1 and Swi3 SWIRM structures are more similar to the LSD1 structure than the Ada2alpha structure. The SWIRM domains of MYSM1 and LSD1 lacked DNA binding activity, while those of Ada2alpha and the human Swi3 counterpart, SMARCC2, bound DNA. The dissimilarity in the DNA-binding ability of the MYSM1 and SMARCC2 SWIRM domains might be due to a couple of amino acid differences in the last helix. These results indicate that the SWIRM family has indeed diverged into three structural subfamilies (Swi3/MYSM1, LSD1, and Ada2 types), and that the Swi3/MYSM1-type subfamily has further diverged into two functionally distinct groups. We also solved the structure of the SANT domain of MYSM1, and demonstrated that it bound DNA with a similar mode to that of the c-Myb DNA-binding domain.

PubMed: 17428495
DOI: 10.1016/j.jmb.2007.03.027

実験手法

SOLUTION NMR