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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery Jasmeen Oberoi , Louise Fairall , Peter J. Watson , Ji-Chun Yang , Zsolt Czimmerer , Thorsten Kampmann , Ben Goult , Jacquie Greenwood , John T. Gooch , Bettina C. Kallenburger , Laszlo Nagy , David Neuhaus , John W. R. Schwabe Nature Structural & Molecular Biology 18 (2), 177 - 184 DOI: 10.1038/nsmb.1983 PMID: 21240272 Diamond Proposal Number(s): [6388] Show Abstract ▼ 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.	Jan 2011

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I03-Macromolecular Crystallography
I04-Macromolecular Crystallography

Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery