2MWI

The structure of the carboxy-terminal domain of DNTTIP1

Summary for 2MWI

• Entry DOI: 10.2210/pdb2mwi/pdb
• NMR Information: BMRB: 25326
• Descriptor: Deoxynucleotidyltransferase terminal-interacting protein 1 (1 entity in total)
• Functional Keywords: hdac, histone deacetylase, gene expression, dnttip1, mideas, hdac1, tdif1, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9H147
• Total number of polymer chains: 1
• Total formula weight: 14060.20

Authors

Schwabe, J.W.R.,Muskett, F.W.,Itoh, T. (deposition date: 2014-11-11, release date: 2015-02-18, Last modification date: 2024-05-01)

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.
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., 43:2033-2044, 2015

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: 25653165
DOI: 10.1093/nar/gkv068

Experimental method

SOLUTION NMR