2n39 - Revision history

OCA at 06:14, 15 May 2024

OCA — Wed, 15 May 2024 06:14:10 GMT

←Older revision		Revision as of 06:14, 15 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2N39 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2N39 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n39 OCA], [https://pdbe.org/2n39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n39 RCSB], [https://www.ebi.ac.uk/pdbsum/2n39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n39 OCA], [https://pdbe.org/2n39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n39 RCSB], [https://www.ebi.ac.uk/pdbsum/2n39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 08:15, 8 March 2023

OCA — Wed, 08 Mar 2023 08:15:07 GMT

←Older revision		Revision as of 08:15, 8 March 2023
Line 1:		Line 1:

	==NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1==		==NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1==
-	<StructureSection load='2n39' size='340' side='right'caption='[[2n39~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2n39' size='340' side='right'caption='[[2n39]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2N39 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2N39 FirstGlance]. <br>
-	</td></tr>~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CHD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n39 OCA], [https://pdbe.org/2n39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n39 RCSB], [https://www.ebi.ac.uk/pdbsum/2n39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n39 OCA], [https://pdbe.org/2n39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n39 RCSB], [https://www.ebi.ac.uk/pdbsum/2n39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://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>	+	[https://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Mackay~~, J P~~]]	+	[[Category: Mackay JP]]
-	[[Category: Mohanty, B]]	+	[[Category: Mohanty B]]
-	[[Category: Ryan~~, D P~~]]	+	[[Category: Ryan DP]]
-	[[Category: Silva~~, A P.G]]~~	+	[[Category: Silva APG]]
-	~~[[Category: C-terminal domain]]~~	+
-	~~[[Category: Chd1]]~~	+
-	~~[[Category: Chromatin remodelling]]~~	+
-	~~[[Category: Dna binding protein]]~~	+
-	~~[[Category: Nucleosome~~]]	+

OCA at 15:26, 2 June 2021

OCA — Wed, 02 Jun 2021 15:26:12 GMT

←Older revision		Revision as of 15:26, 2 June 2021
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	==NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1==		==NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1==
-	<StructureSection load='2n39' size='340' side='right' caption='[[2n39]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2n39' size='340' side='right'caption='[[2n39]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. 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>	+	<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2N39 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CHD1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CHD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n39 OCA], [https://pdbe.org/2n39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n39 RCSB], [https://www.ebi.ac.uk/pdbsum/2n39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~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>	+	[[https://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:

	==See Also==		==See Also==
-	*[[Chromodomain-helicase-DNA-binding protein\|Chromodomain-helicase-DNA-binding protein]]	+	*[[Chromodomain-helicase-DNA-binding protein 3D structures\|Chromodomain-helicase-DNA-binding protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Mackay, J P]]		[[Category: Mackay, J P]]
	[[Category: Mohanty, B]]		[[Category: Mohanty, B]]

OCA at 10:07, 13 February 2019

OCA — Wed, 13 Feb 2019 10:07:42 GMT

←Older revision		Revision as of 10:07, 13 February 2019
Line 3:		Line 3:
	<StructureSection load='2n39' size='340' side='right' caption='[[2n39]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2n39' size='340' side='right' caption='[[2n39]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<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>	+	<table><tr><td colspan='2'>[[2n39]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
-	</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CHD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Mackay, J P]]		[[Category: Mackay, J P]]
	[[Category: Mohanty, B]]		[[Category: Mohanty, B]]

OCA at 06:15, 10 May 2017

OCA — Wed, 10 May 2017 06:15:31 GMT

←Older revision		Revision as of 06:15, 10 May 2017
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<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>		<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>
-	</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>	+	</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n39 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[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>		[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The packaging of eukaryotic DNA into nucleosomes, and the organisation of these nucleosomes into chromatin, plays a critical role in regulating all DNA-associated processes. Chromodomain helicase DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin remodelling protein that is conserved throughout eukaryotes and has an ability to assemble and organise nucleosomes both in vitro and in vivo. This activity is involved in the regulation of transcription and is implicated in mammalian development and stem cell biology. CHD1 is classically depicted as possessing a pair of tandem chromodomains that directly precede a core catalytic helicase-like domain that is then followed by a SANT-SLIDE DNA-binding domain. Here, we have identified an additional conserved domain C-terminal to the SANT-SLIDE domain and determined its structure by multidimensional heteronuclear NMR spectroscopy. We have termed this domain the CHD1 helical C-terminal (CHCT) domain as it is comprised of five alpha-helices arranged in a variant helical bundle topology. CHCT has a conserved, positively charged surface and is able to bind DNA and nucleosomes. In addition, we have identified another group of proteins, the as yet uncharacterised C17orf64 proteins, as also containing a conserved CHCT domain. Our data provide new structural insights into the CHD1 enzyme family.
		+
		+	The Chromatin Remodelling Protein CHD1 Contains a Previously Unrecognised C-Terminal Helical Domain.,Mohanty B, Helder S, Silva AP, Mackay JP, Ryan DP J Mol Biol. 2016 Oct 23;428(21):4298-4314. doi: 10.1016/j.jmb.2016.08.028. Epub, 2016 Aug 31. PMID:27591891<ref>PMID:27591891</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 2n39" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Chromodomain-helicase-DNA-binding protein\|Chromodomain-helicase-DNA-binding protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:02, 2 June 2016

OCA — Thu, 02 Jun 2016 06:02:44 GMT

←Older revision		Revision as of 06:02, 2 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 2n39 ~~is ON HOLD until Paper Publication~~	+	==NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1==
-		+	<StructureSection load='2n39' size='340' side='right' caption='[[2n39]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~Authors~~: ~~Mohanty, B~~., ~~Silva, A~~.P.G., ~~Mackay~~, J.P., ~~Ryan, D~~.P.	+	== Structural highlights ==
-		+	<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>
-	~~Description~~: ~~NMR solution structure of a C~~-~~terminal domain~~ of the ~~chromodomain helicase~~ DNA-~~binding protein 1~~	+	</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>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Mackay, J P]]
	[[Category: Mohanty, B]]		[[Category: Mohanty, B]]
-	[[Category: Silva, A.P.G]]	+	[[Category: Ryan, D P]]
-	[[Category: ~~Mackay, J.P~~]]	+	[[Category: Silva, A P.G]]
-	[[Category: ~~Ryan, D.P~~]]	+	[[Category: C-terminal domain]]
		+	[[Category: Chd1]]
		+	[[Category: Chromatin remodelling]]
		+	[[Category: Dna binding protein]]
		+	[[Category: Nucleosome]]

OCA at 09:25, 17 June 2015

OCA — Wed, 17 Jun 2015 09:25:29 GMT

←Older revision		Revision as of 09:25, 17 June 2015
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2n39 is ON HOLD	+	The entry 2n39 is ON HOLD until Paper Publication

	Authors: Mohanty, B., Silva, A.P.G., Mackay, J.P., Ryan, D.P.		Authors: Mohanty, B., Silva, A.P.G., Mackay, J.P., Ryan, D.P.

OCA: Protected "2n39" [edit=sysop:move=sysop]

OCA — Wed, 03 Jun 2015 07:19:00 GMT

Protected "2n39" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:19, 3 June 2015

OCA: New page: '''Unreleased structure''' The entry 2n39 is ON HOLD Authors: Mohanty, B., Silva, A.P.G., Mackay, J.P., Ryan, D.P. Description: NMR solution structure of a C-terminal domain of the chr...

OCA — Wed, 03 Jun 2015 07:18:59 GMT

New page: '''Unreleased structure''' The entry 2n39 is ON HOLD Authors: Mohanty, B., Silva, A.P.G., Mackay, J.P., Ryan, D.P. Description: NMR solution structure of a C-terminal domain of the chr...

New page

'''Unreleased structure'''

The entry 2n39 is ON HOLD

Authors: Mohanty, B., Silva, A.P.G., Mackay, J.P., Ryan, D.P.

Description: NMR solution structure of a C-terminal domain of the chromodomain helicase DNA-binding protein 1
[[Category: Unreleased Structures]]
[[Category: Mohanty, B]]
[[Category: Silva, A.P.G]]
[[Category: Mackay, J.P]]
[[Category: Ryan, D.P]]