5fxy

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'''Unreleased structure'''
 
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The entry 5fxy is ON HOLD until Paper Publication
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==Structure of the human RBBP4:MTA1(464-546) complex==
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<StructureSection load='5fxy' size='340' side='right' caption='[[5fxy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5fxy]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FXY 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=5fxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fxy OCA], [http://pdbe.org/5fxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fxy RCSB], [http://www.ebi.ac.uk/pdbsum/5fxy PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://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> [[http://www.uniprot.org/uniprot/MTA1_HUMAN MTA1_HUMAN]] May be involved in the regulation of gene expression by covalent modification of histone proteins. Isoform Long is a corepressor of estrogen receptor (ER). Isoform Short binds to ER and sequesters it in the cytoplasm and enhances non-genomic responses of ER.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The NuRD complex is a multi-protein transcriptional corepressor that couples histone deacetylase and ATP-dependent chromatin remodelling activities. The complex regulates the higher-order structure of chromatin, and has important roles in the regulation of gene expression, DNA damage repair and cell differentiation. HDACs 1 and 2 are recruited by the MTA1 corepressor to form the catalytic core of the complex. The histone chaperone protein RBBP4, has previously been shown to bind to the carboxy-terminal tail of MTA1. We show that MTA1 recruits a second copy of RBBP4. The crystal structure reveals an extensive interface between MTA1 and RBBP4. An EM structure, supported by SAXS and crosslinking, reveals the architecture of the dimeric HDAC1:MTA1:RBBP4 assembly which forms the core of the NuRD complex. We find evidence that in this complex RBBP4 mediates interaction with histone H3 tails, but not histone H4, suggesting a mechanism for recruitment of the NuRD complex to chromatin.
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Authors:
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The structure of the core NuRD repression complex provides insights into its interaction with chromatin.,Millard CJ, Varma N, Saleh A, Morris K, Watson PJ, Bottrill AR, Fairall L, Smith CJ, Schwabe JW Elife. 2016 Apr 21;5. pii: e13941. doi: 10.7554/eLife.13941. PMID:27098840<ref>PMID:27098840</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5fxy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Fairall, L]]
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[[Category: Millard, C J]]
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[[Category: Schwabe, J W.R]]
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[[Category: Varma, N]]
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[[Category: Transcription]]
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[[Category: Transcription repression complex metastasis associated complex mta1 rbbp4 rbbp7 histone binding protein]]

Revision as of 08:13, 1 June 2016

Structure of the human RBBP4:MTA1(464-546) complex

5fxy, resolution 3.20Å

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