2mwi

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'''Unreleased structure'''
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==The structure of the carboxy-terminal domain of DNTTIP1==
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<StructureSection load='2mwi' size='340' side='right' caption='[[2mwi]], [[NMR_Ensembles_of_Models | 65 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mwi]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MWI FirstGlance]. <br>
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</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=2mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mwi RCSB], [http://www.ebi.ac.uk/pdbsum/2mwi PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 2mwi is ON HOLD until Paper Publication
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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>
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Authors: Schwabe, J.W.R., Muskett, F.W., Itoh, T.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: The structure of the carboxy-terminal domain of DNTTIP1
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Muskett, F.W]]
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__TOC__
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</StructureSection>
[[Category: Itoh, T]]
[[Category: Itoh, T]]
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[[Category: Schwabe, J.W.R]]
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[[Category: Muskett, F W]]
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[[Category: Schwabe, J W.R]]
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[[Category: Dnttip1]]
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[[Category: Gene expression]]
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[[Category: Hdac]]
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[[Category: Hdac1]]
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[[Category: Histone deacetylase]]
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[[Category: Midea]]
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[[Category: Protein binding]]
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[[Category: Tdif1]]

Revision as of 13:03, 18 February 2015

The structure of the carboxy-terminal domain of DNTTIP1

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