5yx2

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'''Unreleased structure'''
 
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The entry 5yx2 is ON HOLD until Paper Publication
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==Crystal structure of DNMT3A-DNMT3L in complex with DNA containing two CpG sites==
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<StructureSection load='5yx2' size='340' side='right' caption='[[5yx2]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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Authors: Zhang, Z.M., Song, J.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yx2]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YX2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YX2 FirstGlance]. <br>
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Description: Crystal structure of DNMT3A-DNMT3L in complex with DNA containing two CpG sites
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYO:1-(BETA-D-RIBOFURANOSYL)-PYRIMIDIN-2-ONE-5-PHOSPHATE'>PYO</scene></td></tr>
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<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>
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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=5yx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yx2 OCA], [http://pdbe.org/5yx2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yx2 RCSB], [http://www.ebi.ac.uk/pdbsum/5yx2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yx2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/DNM3A_HUMAN DNM3A_HUMAN]] Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZNF238. Can actively repress transcription through the recruitment of HDAC activity (By similarity).<ref>PMID:16357870</ref> [[http://www.uniprot.org/uniprot/DNM3L_HUMAN DNM3L_HUMAN]] Catalytically inactive regulatory factor of DNA methyltransferases. It is essential for the function of DNMT3A and DNMT3B. Activates DNMT3A and DNMT3B by binding to their catalytic domain. Accelerates the binding of DNA and AdoMet to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases. Recognizes unmethylated histone H3 lysine 4 (H3K4) and induces de novo DNA methylation by recruitment or activation of DNMT3.<ref>PMID:17687327</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Song, J]]
[[Category: Song, J]]
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[[Category: Zhang, Z.M]]
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[[Category: Zhang, Z M]]
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[[Category: Dna methylation]]
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[[Category: Dnmt3a]]
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[[Category: Dnmt3l]]
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[[Category: Transferase-transferase regulator-dna complex]]

Revision as of 05:55, 31 January 2018

Crystal structure of DNMT3A-DNMT3L in complex with DNA containing two CpG sites

5yx2, resolution 2.65Å

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