3CEY
Crystal structure of L3MBTL2
3CEY の概要
| エントリーDOI | 10.2210/pdb3cey/pdb |
| 分子名称 | Lethal(3)malignant brain tumor-like 2 protein (2 entities in total) |
| 機能のキーワード | mbt, structural genomics, structural genomics consortium, sgc, chromatin regulator, metal-binding, nucleus, transcription, transcription regulation, zinc-finger, transcription regulator |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Nucleus (Probable): Q969R5 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 108694.76 |
| 構造登録者 | Nady, N.,Guo, Y.,Pan, P.,Allali-Hassani, A.,Qi, C.,Zhu, H.,Dong, A.,Mackenzie, F.,Crombet, L.,Loppnau, P.,Kozieradzki, I.,Vedadi, M.,Edwards, A.M.,Weigelt, J.,Bountra, C.,Arrowsmith, C.H.,Bochkarev, A.,Read, R.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2008-02-29, 公開日: 2008-05-06, 最終更新日: 2024-11-13) |
| 主引用文献 | Guo, Y.,Nady, N.,Qi, C.,Allali-Hassani, A.,Zhu, H.,Pan, P.,Adams-Cioaba, M.A.,Amaya, M.F.,Dong, A.,Vedadi, M.,Schapira, M.,Read, R.J.,Arrowsmith, C.H.,Min, J. Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2. Nucleic Acids Res., 37:2204-2210, 2009 Cited by PubMed Abstract: The MBT repeat has been recently identified as a key domain capable of methyl-lysine histone recognition. Functional work has pointed to a role for MBT domain-containing proteins in transcriptional repression of developmental control genes such as Hox genes. In this study, L3MBTL2, a human homolog of Drosophila Sfmbt critical for Hox gene silencing, is demonstrated to preferentially recognize lower methylation states of several histone-derived peptides through its fourth MBT repeat. High-resolution crystallographic analysis of the four MBT repeats of this protein reveals its unique asymmetric rhomboid architecture, as well as binding mechanism, which preclude the interaction of the first three MBT repeats with methylated peptides. Structural elucidation of an L3MBTL2-H4K20me1 complex and comparison with other MBT-histone peptide complexes also suggests that an absence of distinct surface contours surrounding the methyl-lysine-binding pocket may underlie the lack of sequence specificity observed for members of this protein family. PubMed: 19233876DOI: 10.1093/nar/gkp086 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






