2L5G

Co-ordinates and 1H, 13C and 15N chemical shift assignments for the complex of GPS2 53-90 and SMRT 167-207

2L5G の概要

• エントリーDOI: 10.2210/pdb2l5g/pdb
• NMR情報: BMRB: 17271
• 分子名称: G protein pathway suppressor 2, Putative uncharacterized protein NCOR2 (2 entities in total)
• 機能のキーワード: gps2, smrt, tbl1, co-repressor, transcription regulator
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9641.16

構造登録者

Oberoi, J.,Yang, J.,Neuhaus, D.,Schwabe, J.W.R. (登録日: 2010-11-01, 公開日: 2011-02-02, 最終更新日: 2024-05-01)

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.
Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery.
Nat.Struct.Mol.Biol., 18:177-184, 2011

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: 21240272
DOI: 10.1038/nsmb.1983

実験手法

SOLUTION NMR