4cck: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cck]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCK FirstGlance]. <br> | <table><tr><td colspan='2'>[[4cck]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCK FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdv|2xdv]], [[4bu2|4bu2]], [[4bxf|4bxf]], [[4ccj|4ccj]], [[4ccm|4ccm]], [[4ccn|4ccn]], [[4cco|4cco]], [[4diq|4diq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdv|2xdv]], [[4bu2|4bu2]], [[4bxf|4bxf]], [[4ccj|4ccj]], [[4ccm|4ccm]], [[4ccn|4ccn]], [[4cco|4cco]], [[4diq|4diq]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cck RCSB], [http://www.ebi.ac.uk/pdbsum/4cck 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=4cck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cck OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cck RCSB], [http://www.ebi.ac.uk/pdbsum/4cck PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/NO66_HUMAN NO66_HUMAN]] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</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: Chowdhury, R | [[Category: Chowdhury, R]] | ||
[[Category: Clifton, I J | [[Category: Clifton, I J]] | ||
[[Category: Ge, W | [[Category: Ge, W]] | ||
[[Category: Schofield, C J | [[Category: Schofield, C J]] | ||
[[Category: 2-oxoglutarate]] | [[Category: 2-oxoglutarate]] | ||
[[Category: Beta-hydroxylation]] | [[Category: Beta-hydroxylation]] | ||