4pc0

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pc0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pc0 PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pc0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pc0 PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Nucleosome Remodeling and Deacetylase (NuRD) complex is a widely conserved transcriptional co-regulator that harbors both nucleosome remodeling and histone deacetylase activities. It plays a critical role in the early stages of ES cell differentiation and the reprogramming of somatic to induced pluripotent stem cells. Abnormalities in several NuRD proteins are associated with cancer and ageing. We have investigated the architecture of NuRD by determining the structure of a sub-complex comprising RbAp48 and MTA1. Surprisingly, RbAp48 recognizes MTA1 using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46/48 interactions with histones. Taken together with other results, our data shows that the MTA proteins act as scaffolds for NuRD complex assembly. We further show that the RbAp48-MTA1 interaction is essential for the in vivo integration of RbAp46/48 into the NuRD complex.
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Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 sub-complex.,Alqarni SS, Murthy A, Zhang W, Przewloka MR, Silva AP, Watson AA, Lejon S, Pei XY, Smits AH, Kloet SL, Wang H, Shepherd NE, Stokes PH, Blobel GA, Vermeulen M, Glover DM, Mackay JP, Laue ED J Biol Chem. 2014 Jun 11. pii: jbc.M114.558940. PMID:24920672<ref>PMID:24920672</ref>
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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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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 05:27, 25 June 2014

Structure of the human RbAp48-MTA1(670-711) complex

4pc0, resolution 2.50Å

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