4D6K
Structure of DNTTIP1 dimerisation domain.
Summary for 4D6K
| Entry DOI | 10.2210/pdb4d6k/pdb |
| Descriptor | DEOXYNUCLEOTIDYLTRANSFERASE TERMINAL-INTERACTING PROTEIN 1 (2 entities in total) |
| Functional Keywords | transcription, hdac1, mideas, histone deacetylase complex, tdif1 |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 6 |
| Total formula weight | 62549.72 |
| Authors | Itoh, T.,Fairall, L.,Schwabe, J.W.R. (deposition date: 2014-11-11, release date: 2015-02-18, Last modification date: 2024-05-08) |
| Primary citation | Itoh, T.,Fairall, L.,Muskett, F.W.,Milano, C.P.,Watson, P.J.,Arnaudo, N.,Saleh, A.,Millard, C.J.,El-Mezgueldi, M.,Martino, F.,Schwabe, J.W.R. Structural and Functional Characterization of a Cell Cycle Associated Hdac1/2 Complex Reveals the Structural Basis for Complex Assembly and Nucleosome Targeting. Nucleic Acids Res., 43:2033-, 2015 Cited by PubMed Abstract: Recent proteomic studies have identified a novel histone deacetylase complex that is upregulated during mitosis and is associated with cyclin A. This complex is conserved from nematodes to man and contains histone deacetylases 1 and 2, the MIDEAS corepressor protein and a protein called DNTTIP1 whose function was hitherto poorly understood. Here, we report the structures of two domains from DNTTIP1. The amino-terminal region forms a tight dimerization domain with a novel structural fold that interacts with and mediates assembly of the HDAC1:MIDEAS complex. The carboxy-terminal domain of DNTTIP1 has a structure related to the SKI/SNO/DAC domain, despite lacking obvious sequence homology. We show that this domain in DNTTIP1 mediates interaction with both DNA and nucleosomes. Thus, DNTTIP1 acts as a dimeric chromatin binding module in the HDAC1:MIDEAS corepressor complex. PubMed: 25653165DOI: 10.1093/NAR/GKV068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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