2n39

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'''Unreleased structure'''
 
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The entry 2n39 is ON HOLD until Paper Publication
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==NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1==
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<StructureSection load='2n39' size='340' side='right' caption='[[2n39]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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Authors: Mohanty, B., Silva, A.P.G., Mackay, J.P., Ryan, D.P.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N39 FirstGlance]. <br>
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Description: NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1
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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=2n39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n39 OCA], [http://pdbe.org/2n39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n39 RCSB], [http://www.ebi.ac.uk/pdbsum/2n39 PDBsum]</span></td></tr>
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[[Category: Unreleased Structures]]
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CHD1_HUMAN CHD1_HUMAN]] ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells.<ref>PMID:18042460</ref>
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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: Mackay, J P]]
[[Category: Mohanty, B]]
[[Category: Mohanty, B]]
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[[Category: Silva, A.P.G]]
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[[Category: Ryan, D P]]
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[[Category: Mackay, J.P]]
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[[Category: Silva, A P.G]]
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[[Category: Ryan, D.P]]
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[[Category: C-terminal domain]]
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[[Category: Chd1]]
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[[Category: Chromatin remodelling]]
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[[Category: Dna binding protein]]
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[[Category: Nucleosome]]

Revision as of 06:02, 2 June 2016

NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1

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