6mm1: Difference between revisions

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'''Unreleased structure'''


The entry 6mm1 is ON HOLD  until Paper Publication
==Structure of the cysteine-rich region from human EHMT2==
 
<StructureSection load='6mm1' size='340' side='right'caption='[[6mm1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
Authors: Kerchner, K.M., Mou, T.C., Sprang, S.R., Briknarova, K.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6mm1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MM1 FirstGlance]. <br>
Description: Structure of the cysteine-rich region from human EHMT2
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Unreleased Structures]]
<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=6mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mm1 OCA], [http://pdbe.org/6mm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mm1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mm1 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/EHMT2_HUMAN EHMT2_HUMAN]] Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.<ref>PMID:8457211</ref> <ref>PMID:11316813</ref> <ref>PMID:18438403</ref> <ref>PMID:20118233</ref> <ref>PMID:22387026</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Briknarova, K]]
[[Category: Briknarova, K]]
[[Category: Mou, T.C]]
[[Category: Kerchner, K M]]
[[Category: Kerchner, K.M]]
[[Category: Mou, T C]]
[[Category: Sprang, S.R]]
[[Category: Sprang, S R]]
[[Category: Cysteine-rich region]]
[[Category: Ring-like]]
[[Category: Transferase]]
[[Category: Zinc-binding]]

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