3rvh
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rvh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RVH FirstGlance]. <br> | <table><tr><td colspan='2'>[[3rvh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RVH FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HQ2:8-HYDROXY-3-(PIPERAZIN-1-YL)QUINOLINE-5-CARBOXYLIC+ACID'>HQ2</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </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=HQ2:8-HYDROXY-3-(PIPERAZIN-1-YL)QUINOLINE-5-CARBOXYLIC+ACID'>HQ2</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oq7|2oq7]], [[2ox0|2ox0]], [[2vd7|2vd7]], [[2wwj|2wwj]], [[3njy|3njy]], [[3pdq|3pdq]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oq7|2oq7]], [[2ox0|2ox0]], [[2vd7|2vd7]], [[2wwj|2wwj]], [[3njy|3njy]], [[3pdq|3pdq]]</td></tr> |
- | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">JHDM3A, JMJD2, JMJD2A, KDM4A, KIAA0677 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">JHDM3A, JMJD2, JMJD2A, KDM4A, KIAA0677 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3rvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rvh RCSB], [http://www.ebi.ac.uk/pdbsum/3rvh 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=3rvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rvh RCSB], [http://www.ebi.ac.uk/pdbsum/3rvh PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Jumonji domain-containing protein 2A|Jumonji domain-containing protein 2A]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Clifton, I J | + | [[Category: Clifton, I J]] |
- | [[Category: Heightman, T D | + | [[Category: Heightman, T D]] |
- | [[Category: Jadhav, A | + | [[Category: Jadhav, A]] |
- | [[Category: King, O N.F | + | [[Category: King, O N.F]] |
- | [[Category: Maloney, D J | + | [[Category: Maloney, D J]] |
- | [[Category: McDonough, M A | + | [[Category: McDonough, M A]] |
- | [[Category: Rai, G | + | [[Category: Rai, G]] |
- | [[Category: Schofield, C J | + | [[Category: Schofield, C J]] |
- | [[Category: Simeonov, A | + | [[Category: Simeonov, A]] |
- | [[Category: Tumber, A | + | [[Category: Tumber, A]] |
[[Category: 2-oxoglutarate]] | [[Category: 2-oxoglutarate]] | ||
[[Category: Alpha-ketoglutarate]] | [[Category: Alpha-ketoglutarate]] |
Revision as of 03:14, 25 December 2014
Crystal Structure of JMJD2A Complexed with Inhibitor
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Categories: Homo sapiens | Clifton, I J | Heightman, T D | Jadhav, A | King, O N.F | Maloney, D J | McDonough, M A | Rai, G | Schofield, C J | Simeonov, A | Tumber, A | 2-oxoglutarate | Alpha-ketoglutarate | Chromatin regulator | Demethylation | Dioxygenase | Iron | Jmjc domain | Nucleus | Oxidoreductase | Oxidoreductase-oxidoreductase inhibitor complex | Transcription