4wxx - Revision history

OCA at 12:59, 1 March 2024

OCA — Fri, 01 Mar 2024 12:59:22 GMT

←Older revision		Revision as of 12:59, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4wxx]] is a 2 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=4WXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXX FirstGlance]. <br>		<table><tr><td colspan='2'>[[4wxx]] is a 2 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=4WXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.622Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [https://pdbe.org/4wxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [https://www.ebi.ac.uk/pdbsum/4wxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxx 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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [https://pdbe.org/4wxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [https://www.ebi.ac.uk/pdbsum/4wxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxx ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN] Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9.<ref>PMID:16357870</ref> <ref>PMID:18754681</ref> <ref>PMID:18413740</ref>		[https://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN] Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9.<ref>PMID:16357870</ref> <ref>PMID:18754681</ref> <ref>PMID:18413740</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DNMT1 (DNA methyltransferase 1) is responsible for propagating the DNA methylation patterns during DNA replication. DNMT1 contains, in addition to a C-terminal methyltransferase domain, a large N-terminal regulatory region that is composed of an RFTS (replication foci targeting sequence) domain, a CXXC zinc finger domain and a pair of BAH (bromo adjacent homology) domains. The regulatory domains of DNMT1 mediate a network of protein-protein and protein-DNA interactions to control the recruitment and enzymatic activity of DNMT1. Here we report the crystal structure of human DNMT1 with all the structural domains (hDNMT1, residues 351-1600) in complex with S-adenosyl-l-homocysteine at 2.62A resolution. The RFTS domain directly associates with the methyltransferase domain, thereby inhibiting the substrate binding of hDNMT1. Through structural analysis, mutational, biochemical and enzymatic studies, we further identify that a linker sequence between the CXXC and BAH1 domains, aside from its role in the CXXC domain-mediated DNMT1 autoinhibition, serves as an important regulatory element in the RFTS domain-mediated autoinhibition. In comparison with the previously determined structure of mouse DNMT1, this study also reveals a number of distinct structural features that may underlie subtle functional diversity observed for the two orthologues. In addition, this structure provides a framework for understanding the functional consequence of disease-related hDNMT1 mutations.
-
-	Crystal Structure of Human DNA Methyltransferase 1.,Zhang ZM, Liu S, Lin K, Luo Y, Perry JJ, Wang Y, Song J J Mol Biol. 2015 Jun 10. pii: S0022-2836(15)00341-1. doi:, 10.1016/j.jmb.2015.06.001. PMID:26070743<ref>PMID:26070743</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4wxx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 21:03, 12 April 2023

OCA — Wed, 12 Apr 2023 21:03:01 GMT

←Older revision		Revision as of 21:03, 12 April 2023
Line 3:		Line 3:
	<StructureSection load='4wxx' size='340' side='right'caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>		<StructureSection load='4wxx' size='340' side='right'caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wxx]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4WXX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wxx]] is a 2 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=4WXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DNMT1, AIM, CXXC9, DNMT ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [https://pdbe.org/4wxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [https://www.ebi.ac.uk/pdbsum/4wxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxx ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span></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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [~~http~~://pdbe.org/4wxx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4wxx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxx ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN]] Defects in DNMT1 are the cause of hereditary sensory neuropathy type 1E (HSN1E) [MIM:[~~http~~://omim.org/entry/614116 614116]]. A neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia.<ref>PMID:21532572</ref>	+	[https://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN] Defects in DNMT1 are the cause of hereditary sensory neuropathy type 1E (HSN1E) [MIM:[https://omim.org/entry/614116 614116]. A neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia.<ref>PMID:21532572</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN]] Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9.<ref>PMID:16357870</ref> <ref>PMID:18754681</ref> <ref>PMID:18413740</ref>	+	[https://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN] Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9.<ref>PMID:16357870</ref> <ref>PMID:18754681</ref> <ref>PMID:18413740</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:

	==See Also==		==See Also==
-	*[[DNA methyltransferase\|DNA methyltransferase]]	+	*[[DNA methyltransferase 3D structures\|DNA methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Song, J]]	+	[[Category: Song J]]
-	[[Category: Zhang~~, Z M]]~~	+	[[Category: Zhang ZM]]
-	~~[[Category: Dna methylation]]~~	+
-	~~[[Category: Dna methytransferase1]]~~	+
-	~~[[Category: Dnmt1]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:07, 23 May 2019

OCA — Thu, 23 May 2019 08:07:17 GMT

←Older revision		Revision as of 08:07, 23 May 2019
Line 1:		Line 1:

	==The crystal structure of human DNMT1(351-1600)==		==The crystal structure of human DNMT1(351-1600)==
-	<StructureSection load='4wxx' size='340' side='right' caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>	+	<StructureSection load='4wxx' size='340' side='right'caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wxx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wxx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DNMT1, AIM, CXXC9, DNMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span></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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [http://pdbe.org/4wxx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [http://www.ebi.ac.uk/pdbsum/4wxx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxx ProSAT]</span></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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [http://pdbe.org/4wxx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [http://www.ebi.ac.uk/pdbsum/4wxx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxx ProSAT]</span></td></tr>
Line 28:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Song, J]]		[[Category: Song, J]]
	[[Category: Zhang, Z M]]		[[Category: Zhang, Z M]]

OCA at 13:24, 10 May 2017

OCA — Wed, 10 May 2017 13:24:20 GMT

←Older revision		Revision as of 13:24, 10 May 2017
Line 1:		Line 1:
		+
	==The crystal structure of human DNMT1(351-1600)==		==The crystal structure of human DNMT1(351-1600)==
	<StructureSection load='4wxx' size='340' side='right' caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>		<StructureSection load='4wxx' size='340' side='right' caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span></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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [http://www.ebi.ac.uk/pdbsum/4wxx PDBsum]</span></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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [http://pdbe.org/4wxx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [http://www.ebi.ac.uk/pdbsum/4wxx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxx ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4wxx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[DNA methyltransferase\|DNA methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:26, 22 July 2015

OCA — Wed, 22 Jul 2015 08:26:12 GMT

←Older revision		Revision as of 08:26, 22 July 2015
Line 1:		Line 1:
-	==The crystal structure of human DNMT1(351-1600) ~~at 2.62 Angstroms resolution~~==	+	==The crystal structure of human DNMT1(351-1600)==
	<StructureSection load='4wxx' size='340' side='right' caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>		<StructureSection load='4wxx' size='340' side='right' caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 13:26, 15 July 2015

OCA — Wed, 15 Jul 2015 13:26:34 GMT

←Older revision		Revision as of 13:26, 15 July 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution==
		+	<StructureSection load='4wxx' size='340' side='right' caption='[[4wxx]], [[Resolution\|resolution]] 2.62Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4wxx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXX FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span></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=4wxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wxx RCSB], [http://www.ebi.ac.uk/pdbsum/4wxx PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN]] Defects in DNMT1 are the cause of hereditary sensory neuropathy type 1E (HSN1E) [MIM:[http://omim.org/entry/614116 614116]]. A neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia.<ref>PMID:21532572</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DNMT1_HUMAN DNMT1_HUMAN]] Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9.<ref>PMID:16357870</ref> <ref>PMID:18754681</ref> <ref>PMID:18413740</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DNMT1 (DNA methyltransferase 1) is responsible for propagating the DNA methylation patterns during DNA replication. DNMT1 contains, in addition to a C-terminal methyltransferase domain, a large N-terminal regulatory region that is composed of an RFTS (replication foci targeting sequence) domain, a CXXC zinc finger domain and a pair of BAH (bromo adjacent homology) domains. The regulatory domains of DNMT1 mediate a network of protein-protein and protein-DNA interactions to control the recruitment and enzymatic activity of DNMT1. Here we report the crystal structure of human DNMT1 with all the structural domains (hDNMT1, residues 351-1600) in complex with S-adenosyl-l-homocysteine at 2.62A resolution. The RFTS domain directly associates with the methyltransferase domain, thereby inhibiting the substrate binding of hDNMT1. Through structural analysis, mutational, biochemical and enzymatic studies, we further identify that a linker sequence between the CXXC and BAH1 domains, aside from its role in the CXXC domain-mediated DNMT1 autoinhibition, serves as an important regulatory element in the RFTS domain-mediated autoinhibition. In comparison with the previously determined structure of mouse DNMT1, this study also reveals a number of distinct structural features that may underlie subtle functional diversity observed for the two orthologues. In addition, this structure provides a framework for understanding the functional consequence of disease-related hDNMT1 mutations.

-	~~The entry 4wxx is ON HOLD until Paper Publication~~	+	Crystal Structure of Human DNA Methyltransferase 1.,Zhang ZM, Liu S, Lin K, Luo Y, Perry JJ, Wang Y, Song J J Mol Biol. 2015 Jun 10. pii: S0022-2836(15)00341-1. doi:, 10.1016/j.jmb.2015.06.001. PMID:26070743<ref>PMID:26070743</ref>

-	~~Authors: Zhang~~, Z.M.~~, Song, J~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Song, J]]		[[Category: Song, J]]
-	[[Category: Zhang, Z.M]]	+	[[Category: Zhang, Z M]]
		+	[[Category: Dna methylation]]
		+	[[Category: Dna methytransferase1]]
		+	[[Category: Dnmt1]]
		+	[[Category: Transferase]]

OCA at 20:11, 24 December 2014

OCA — Wed, 24 Dec 2014 20:11:09 GMT

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	Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution		Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution
		+	[[Category: Unreleased Structures]]
		+	[[Category: Song, J]]
		+	[[Category: Zhang, Z.M]]

OCA at 11:37, 17 December 2014

OCA — Wed, 17 Dec 2014 11:37:46 GMT

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-	The entry 4wxx is ON HOLD	+	The entry 4wxx is ON HOLD until Paper Publication

	Authors: Zhang, Z.M., Song, J.		Authors: Zhang, Z.M., Song, J.

	Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution		Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution

OCA: Protected "4wxx" [edit=sysop:move=sysop]

OCA — Wed, 26 Nov 2014 07:12:08 GMT

Protected "4wxx" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:12, 26 November 2014

OCA: New page: '''Unreleased structure''' The entry 4wxx is ON HOLD Authors: Zhang, Z.M., Song, J. Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution

OCA — Wed, 26 Nov 2014 07:12:06 GMT

New page: '''Unreleased structure''' The entry 4wxx is ON HOLD Authors: Zhang, Z.M., Song, J. Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution

New page

'''Unreleased structure'''

The entry 4wxx is ON HOLD

Authors: Zhang, Z.M., Song, J.

Description: The crystal structure of human DNMT1(351-1600) at 2.62 Angstroms resolution