2XTD
Structure of the TBL1 tetramerisation domain
2XTD の概要
エントリーDOI | 10.2210/pdb2xtd/pdb |
関連するPDBエントリー | 2XTC 2XTE |
分子名称 | TBL1 F-BOX-LIKE/WD REPEAT-CONTAINING PROTEIN TBL1X (1 entity in total) |
機能のキーワード | transcription, n-cor repressor complex, proteasome |
由来する生物種 | HOMO SAPIENS (HUMAN) |
細胞内の位置 | Nucleus (Probable): O60907 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 15567.20 |
構造登録者 | Oberoi, J.,Fairall, L.,Watson, P.J.,Greenwood, J.A.,Schwabe, J.W.R. (登録日: 2010-10-06, 公開日: 2011-01-19, 最終更新日: 2023-12-20) |
主引用文献 | Oberoi, J.,Fairall, L.,Watson, P.J.,Yang, J.C.,Czimmerer, Z.,Kampmann, T.,Goult, B.T.,Greenwood, J.A.,Gooch, J.T.,Kallenberger, B.C.,Nagy, L.,Neuhaus, D.,Schwabe, J.W.R. Structural Basis for the Assembly of the Smrt/Ncor Core Transcriptional Repression Machinery. Nat.Struct.Mol.Biol., 18:177-, 2011 Cited by PubMed Abstract: Eukaryotic transcriptional repressors function by recruiting large coregulatory complexes that target histone deacetylase enzymes to gene promoters and enhancers. Transcriptional repression complexes, assembled by the corepressor NCoR and its homolog SMRT, are crucial in many processes, including development and metabolic physiology. The core repression complex involves the recruitment of three proteins, HDAC3, GPS2 and TBL1, to a highly conserved repression domain within SMRT and NCoR. We have used structural and functional approaches to gain insight into the architecture and biological role of this complex. We report the crystal structure of the tetrameric oligomerization domain of TBL1, which interacts with both SMRT and GPS2, and the NMR structure of the interface complex between GPS2 and SMRT. These structures, together with computational docking, mutagenesis and functional assays, reveal the assembly mechanism and stoichiometry of the corepressor complex. PubMed: 21240272DOI: 10.1038/NSMB.1983 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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