2COM
The solution structure of the SWIRM domain of human LSD1
Summary for 2COM
| Entry DOI | 10.2210/pdb2com/pdb |
| NMR Information | BMRB: 10011 |
| Descriptor | Lysine-specific histone demethylase 1 (1 entity in total) |
| Functional Keywords | 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 |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: O60341 |
| Total number of polymer chains | 1 |
| Total formula weight | 13727.43 |
| Authors | Tochio, N.,Umehara, T.,Koshiba, S.,Inoue, M.,Tanaka, A.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-05-18, release date: 2005-11-18, Last modification date: 2024-05-29) |
| Primary citation | 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 Cited by 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: 16531230DOI: 10.1016/j.str.2005.12.004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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