4d6k: Difference between revisions

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'''Unreleased structure'''
==Structure of DNTTIP1 dimerisation domain.==
<StructureSection load='4d6k' size='340' side='right' caption='[[4d6k]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4d6k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D6K FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d6k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d6k RCSB], [http://www.ebi.ac.uk/pdbsum/4d6k PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/TDIF1_HUMAN TDIF1_HUMAN]] Shown to enhance TdT activity, in vitro. Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription.<ref>PMID:11473582</ref> <ref>PMID:23874396</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


The entry 4d6k is ON HOLD  until Paper Publication
Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.,Itoh T, Fairall L, Muskett FW, Milano CP, Watson PJ, Arnaudo N, Saleh A, Millard CJ, El-Mezgueldi M, Martino F, Schwabe JW Nucleic Acids Res. 2015 Feb 4. pii: gkv068. PMID:25653165<ref>PMID:25653165</ref>


Authors: Itoh, T., Fairall, L., Schwabe, J.W.R.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Structure of DNTTIP1 dimerisation domain.
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Fairall, L]]
[[Category: Fairall, L]]
[[Category: Itoh, T]]
[[Category: Itoh, T]]
[[Category: Schwabe, J.W.R]]
[[Category: Schwabe, J W.R]]
[[Category: Hdac1]]
[[Category: Histone deacetylase complex]]
[[Category: Midea]]
[[Category: Tdif1]]
[[Category: Transcription]]
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