3pdq - Revision history

OCA at 17:05, 1 November 2023

OCA — Wed, 01 Nov 2023 17:05:51 GMT

←Older revision		Revision as of 17:05, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3pdq' size='340' side='right'caption='[[3pdq]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='3pdq' size='340' side='right'caption='[[3pdq]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3pdq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PDQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3pdq]] 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=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PDQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 1.989Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3njy\|3njy]], [[2wwj\|2wwj]], [[2vd7\|2vd7]], [[2oq7\|2oq7]], [[2ox0\|2ox0]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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">KDM4A ([https://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=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [https://pdbe.org/3pdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [https://www.ebi.ac.uk/pdbsum/3pdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdq 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=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [https://pdbe.org/3pdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [https://www.ebi.ac.uk/pdbsum/3pdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://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>	+	[https://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==		==See Also==
Line 18:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chang, K H]]	+	[[Category: Chang K-H]]
-	[[Category: Clifton~~, I J~~]]	+	[[Category: Clifton IJ]]
-	[[Category: King~~, O N.F~~]]	+	[[Category: King ONF]]
-	[[Category: McDonough~~, M A~~]]	+	[[Category: McDonough MA]]
-	[[Category: Rose~~, N R~~]]	+	[[Category: Rose NR]]
-	[[Category: Schofield~~, C J]]~~	+	[[Category: Schofield CJ]]
-	~~[[Category: 2-oxoglutarate]]~~	+
-	~~[[Category: Alpha-ketoglutarate]]~~	+
-	~~[[Category: Chromatin regulator]]~~	+
-	~~[[Category: Demethylation]]~~	+
-	~~[[Category: Dioxygenase]]~~	+
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Jmjc domain]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 08:35, 25 May 2022

OCA — Wed, 25 May 2022 08:35:15 GMT

←Older revision		Revision as of 08:35, 25 May 2022
Line 1:		Line 1:

	==Crystal structure of JMJD2A complexed with bipyridyl inhibitor==		==Crystal structure of JMJD2A complexed with bipyridyl inhibitor==
-	<StructureSection load='3pdq' size='340' side='right' caption='[[3pdq]], [[Resolution\|resolution]] 1.99Å' scene=''>	+	<StructureSection load='3pdq' size='340' side='right'caption='[[3pdq]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3pdq]] 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=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3PDQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3pdq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PDQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3njy\|3njy]], [[2wwj\|2wwj]], [[2vd7\|2vd7]], [[2oq7\|2oq7]], [[2ox0\|2ox0]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3njy\|3njy]], [[2wwj\|2wwj]], [[2vd7\|2vd7]], [[2oq7\|2oq7]], [[2ox0\|2ox0]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KDM4A ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KDM4A ([https://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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [~~http~~://pdbe.org/3pdq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3pdq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdq 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=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [https://pdbe.org/3pdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [https://www.ebi.ac.uk/pdbsum/3pdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>	+	[[https://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==		==See Also==
-	*[[Jumonji domain-containing protein\|Jumonji domain-containing protein]]	+	*[[Jumonji domain-containing protein 3D structures\|Jumonji domain-containing protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 19:		Line 19:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Chang, K H]]		[[Category: Chang, K H]]
	[[Category: Clifton, I J]]		[[Category: Clifton, I J]]

OCA at 22:26, 5 August 2016

OCA — Fri, 05 Aug 2016 22:26:22 GMT

←Older revision		Revision as of 22:26, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of JMJD2A complexed with bipyridyl inhibitor==		==Crystal structure of JMJD2A complexed with bipyridyl inhibitor==
	<StructureSection load='3pdq' size='340' side='right' caption='[[3pdq]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='3pdq' size='340' side='right' caption='[[3pdq]], [[Resolution\|resolution]] 1.99Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3njy\|3njy]], [[2wwj\|2wwj]], [[2vd7\|2vd7]], [[2oq7\|2oq7]], [[2ox0\|2ox0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3njy\|3njy]], [[2wwj\|2wwj]], [[2vd7\|2vd7]], [[2oq7\|2oq7]], [[2ox0\|2ox0]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KDM4A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KDM4A ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [http://www.ebi.ac.uk/pdbsum/3pdq 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=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [http://pdbe.org/3pdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [http://www.ebi.ac.uk/pdbsum/3pdq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pdq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:

	==See Also==		==See Also==
-	*[[Jumonji domain-containing protein 2A\|Jumonji domain-containing protein 2A]]	+	*[[Jumonji domain-containing protein\|Jumonji domain-containing protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:21, 25 December 2014

OCA — Thu, 25 Dec 2014 06:21:56 GMT

←Older revision		Revision as of 06:21, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3pdq\| PDB=3pdq \| SCENE= }}~~	+	==Crystal structure of JMJD2A complexed with bipyridyl inhibitor==
-	===Crystal structure of JMJD2A complexed with bipyridyl inhibitor===	+	<StructureSection load='3pdq' size='340' side='right' caption='[[3pdq]], [[Resolution\|resolution]] 1.99Å' scene=''>
-		+	== Structural highlights ==
-	==Function==	+	<table><tr><td colspan='2'>[[3pdq]] 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=3PDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PDQ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KC6:4-[(2-AMINOETHYL)CARBAMOYL]-2,2-BIPYRIDINE-4-CARBOXYLIC+ACID'>KC6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3njy\|3njy]], [[2wwj\|2wwj]], [[2vd7\|2vd7]], [[2oq7\|2oq7]], [[2ox0\|2ox0]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KDM4A ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pdq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pdq RCSB], [http://www.ebi.ac.uk/pdbsum/3pdq PDBsum]</span></td></tr>
		+	</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>		[[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>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~3pdq~~]] ~~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=3PDQ OCA].~~	+	*[[Jumonji domain-containing protein 2A\|Jumonji domain-containing protein 2A]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021412984</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Chang, K H.]]	+	[[Category: Chang, K H]]
-	[[Category: Clifton, I J.]]	+	[[Category: Clifton, I J]]
-	[[Category: King, O N.F.]]	+	[[Category: King, O N.F]]
-	[[Category: McDonough, M A.]]	+	[[Category: McDonough, M A]]
-	[[Category: Rose, N R.]]	+	[[Category: Rose, N R]]
-	[[Category: Schofield, C J.]]	+	[[Category: Schofield, C J]]
	[[Category: 2-oxoglutarate]]		[[Category: 2-oxoglutarate]]
	[[Category: Alpha-ketoglutarate]]		[[Category: Alpha-ketoglutarate]]

OCA at 06:45, 26 March 2014

OCA — Wed, 26 Mar 2014 06:45:33 GMT

←Older revision		Revision as of 06:45, 26 March 2014
Line 1:		Line 1:
	{{STRUCTURE_3pdq\| PDB=3pdq \| SCENE= }}		{{STRUCTURE_3pdq\| PDB=3pdq \| SCENE= }}
	===Crystal structure of JMJD2A complexed with bipyridyl inhibitor===		===Crystal structure of JMJD2A complexed with bipyridyl inhibitor===
		+
		+	==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>

	==About this Structure==		==About this Structure==
-	[[3pdq]] 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=3PDQ OCA].	+	[[3pdq]] 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=3PDQ OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:021412984</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:021412984</ref><references group="xtra"/><references/>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Chang, K H.]]		[[Category: Chang, K H.]]
	[[Category: Clifton, I J.]]		[[Category: Clifton, I J.]]

OCA at 08:20, 2 May 2013

OCA — Thu, 02 May 2013 08:20:23 GMT

←Older revision		Revision as of 08:20, 2 May 2013
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-	[[Image:3pdq.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3pdq", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3pdq\| PDB=3pdq \| SCENE= }}		{{STRUCTURE_3pdq\| PDB=3pdq \| SCENE= }}
-
	===Crystal structure of JMJD2A complexed with bipyridyl inhibitor===		===Crystal structure of JMJD2A complexed with bipyridyl inhibitor===
-

	==About this Structure==		==About this Structure==
Line 16:		Line 6:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~21412984~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021412984</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chang, K H.]]		[[Category: Chang, K H.]]
Line 24:		Line 14:
	[[Category: Rose, N R.]]		[[Category: Rose, N R.]]
	[[Category: Schofield, C J.]]		[[Category: Schofield, C J.]]
		+	[[Category: 2-oxoglutarate]]
		+	[[Category: Alpha-ketoglutarate]]
		+	[[Category: Chromatin regulator]]
		+	[[Category: Demethylation]]
		+	[[Category: Dioxygenase]]
		+	[[Category: Iron]]
		+	[[Category: Jmjc domain]]
		+	[[Category: Nucleus]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
		+	[[Category: Transcription]]

OCA: Protected "3pdq" [edit=sysop:move=sysop]

OCA — Wed, 30 Mar 2011 08:08:44 GMT

Protected "3pdq" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:08, 30 March 2011

OCA at 08:08, 30 March 2011

OCA — Wed, 30 Mar 2011 08:08:36 GMT

←Older revision		Revision as of 08:08, 30 March 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:3pdq.jpg\|left\|200px]]

-	The ~~entry 3pdq~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3pdq", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3pdq\| PDB=3pdq \| SCENE= }}

-	~~Authors: King, O.N.F., Chang, K.-H., Rose, N.R., Clifton, I.J., McDonough, M.A., Schofield, C.J.~~	+	===Crystal structure of JMJD2A complexed with bipyridyl inhibitor===

-	Description: Crystal structure of JMJD2A complexed with inhibitor

-	~~''Page seeded by~~ [http://oca.weizmann.ac.il/oca OCA ] ~~on Wed Dec 8 11~~:31:~~39 2010''~~	+	==About this Structure==
		+	[[3pdq]] 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=3PDQ OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:21412984</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Chang, K H.]]
		+	[[Category: Clifton, I J.]]
		+	[[Category: King, O N.F.]]
		+	[[Category: McDonough, M A.]]
		+	[[Category: Rose, N R.]]
		+	[[Category: Schofield, C J.]]

OCA at 08:19, 8 December 2010

OCA — Wed, 08 Dec 2010 08:19:36 GMT

←Older revision		Revision as of 08:19, 8 December 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3pdq is ON HOLD	+	The entry 3pdq is ON HOLD until Paper Publication

	Authors: King, O.N.F., Chang, K.-H., Rose, N.R., Clifton, I.J., McDonough, M.A., Schofield, C.J.		Authors: King, O.N.F., Chang, K.-H., Rose, N.R., Clifton, I.J., McDonough, M.A., Schofield, C.J.
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	Description: Crystal structure of JMJD2A complexed with inhibitor		Description: Crystal structure of JMJD2A complexed with inhibitor

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Nov 18 00~~:33:59 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 8 11:31:39 2010''

OCA at 21:22, 17 November 2010

OCA — Wed, 17 Nov 2010 21:22:44 GMT

←Older revision		Revision as of 21:22, 17 November 2010
Line 3:		Line 3:
	The entry 3pdq is ON HOLD		The entry 3pdq is ON HOLD

-	Authors: King, O.N.F., Chang, K-H., Rose, N.R., Clifton, I.J., McDonough, M.A., Schofield, C.J.	+	Authors: King, O.N.F., Chang, K.-H., Rose, N.R., Clifton, I.J., McDonough, M.A., Schofield, C.J.

	Description: Crystal structure of JMJD2A complexed with inhibitor		Description: Crystal structure of JMJD2A complexed with inhibitor

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed~~ Nov ~~3 10~~:07:57 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Nov 18 00:33:59 2010''