4pby

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==Structure of the human RbAp48-MTA1(656-686) complex==
==Structure of the human RbAp48-MTA1(656-686) complex==
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<StructureSection load='4pby' size='340' side='right' caption='[[4pby]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='4pby' size='340' side='right'caption='[[4pby]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4pby]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PBY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4pby]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PBY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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=4pby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pby OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pby RCSB], [http://www.ebi.ac.uk/pdbsum/4pby PDBsum]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pby OCA], [https://pdbe.org/4pby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pby RCSB], [https://www.ebi.ac.uk/pdbsum/4pby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pby ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RBBP4_HUMAN RBBP4_HUMAN] Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.<ref>PMID:10866654</ref>
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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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==See Also==
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</div>
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*[[Retinoblastoma-binding protein 3D structures|Retinoblastoma-binding protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alqarni, S S.M]]
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[[Category: Homo sapiens]]
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[[Category: Laue, E D]]
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[[Category: Large Structures]]
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[[Category: Lejon, S]]
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[[Category: Alqarni SSM]]
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[[Category: Mackay, J P]]
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[[Category: Laue ED]]
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[[Category: Murthy, A]]
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[[Category: Lejon S]]
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[[Category: Silva, A P.G]]
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[[Category: Mackay JP]]
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[[Category: Watson, A A]]
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[[Category: Murthy A]]
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[[Category: Cell cycle]]
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[[Category: Silva APG]]
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[[Category: Mta1]]
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[[Category: Watson AA]]
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[[Category: Nurd]]
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[[Category: Rbap48]]
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[[Category: Sub-complex]]
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Current revision

Structure of the human RbAp48-MTA1(656-686) complex

PDB ID 4pby

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