2XTD

Structure of the TBL1 tetramerisation domain

Summary for 2XTD

• Entry DOI: 10.2210/pdb2xtd/pdb
• Related: 2XTC 2XTE
• Descriptor: TBL1 F-BOX-LIKE/WD REPEAT-CONTAINING PROTEIN TBL1X (1 entity in total)
• Functional Keywords: transcription, n-cor repressor complex, proteasome
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus (Probable): O60907
• Total number of polymer chains: 2
• Total formula weight: 15567.20

Authors

Oberoi, J.,Fairall, L.,Watson, P.J.,Greenwood, J.A.,Schwabe, J.W.R. (deposition date: 2010-10-06, release date: 2011-01-19, Last modification date: 2023-12-20)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)