4gut - Revision history

OCA at 14:01, 8 November 2023

OCA — Wed, 08 Nov 2023 14:01:41 GMT

←Older revision		Revision as of 14:01, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gut]] 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=4GUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GUT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gut]] 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=4GUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GUT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.998Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [https://pdbe.org/4gut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [https://www.ebi.ac.uk/pdbsum/4gut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gut 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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [https://pdbe.org/4gut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [https://www.ebi.ac.uk/pdbsum/4gut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gut ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:18, 26 October 2022

OCA — Wed, 26 Oct 2022 07:18:35 GMT

←Older revision		Revision as of 07:18, 26 October 2022
Line 1:		Line 1:

	==Crystal structure of LSD2-NPAC==		==Crystal structure of LSD2-NPAC==
-	<StructureSection load='4gut' size='340' side='right' caption='[[4gut]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4gut' size='340' side='right'caption='[[4gut]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gut]] 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=4GUT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GUT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gut]] 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=4GUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GUT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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">[[4gu1\|4gu1]], [[4gur\|4gur]], [[4gus\|4gus]]</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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [https://pdbe.org/4gut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [https://www.ebi.ac.uk/pdbsum/4gut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gut ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LSD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GLYR1 ([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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [~~http~~://pdbe.org/4gut PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gut PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gut ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KDM1B_HUMAN KDM1B_HUMAN]] Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4 (By similarity). [[http://www.uniprot.org/uniprot/GLYR1_HUMAN GLYR1_HUMAN]] May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3).<ref>PMID:16352664</ref> <ref>PMID:20850016</ref>	+	[https://www.uniprot.org/uniprot/KDM1B_HUMAN KDM1B_HUMAN] Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4 (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Lysine-specific histone demethylase\|Lysine-specific histone demethylase]]	+	*[[Lysine-specific histone demethylase 3D structures\|Lysine-specific histone demethylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Chen, F]]	+	[[Category: Large Structures]]
-	[[Category: Dong, Z]]	+	[[Category: Chen F]]
-	[[Category: Fang, J]]	+	[[Category: Dong Z]]
-	[[Category: Fang, R]]	+	[[Category: Fang J]]
-	[[Category: Li, Z]]	+	[[Category: Fang R]]
-	[[Category: Shi, Y]]	+	[[Category: Li Z]]
-	[[Category: Wang, P]]	+	[[Category: Shi Y]]
-	[[Category: Xu, Y]]	+	[[Category: Wang P]]
-	[[Category: Yang, H]]	+	[[Category: Xu Y]]
-	[[Category: Yang, Y]]	+	[[Category: Yang H]]
-	~~[[Category: Histone demethylase]]~~	+	[[Category: Yang Y]]
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 17:59, 5 August 2016

OCA — Fri, 05 Aug 2016 17:59:05 GMT

←Older revision		Revision as of 17:59, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of LSD2-NPAC==		==Crystal structure of LSD2-NPAC==
	<StructureSection load='4gut' size='340' side='right' caption='[[4gut]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4gut' size='340' side='right' caption='[[4gut]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gut]] 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=4GUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GUT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gut]] 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=4GUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GUT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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">[[4gu1\|4gu1]], [[4gur\|4gur]], [[4gus\|4gus]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gu1\|4gu1]], [[4gur\|4gur]], [[4gus\|4gus]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LSD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), GLYR1 ([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">LSD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GLYR1 ([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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [http://www.ebi.ac.uk/pdbsum/4gut 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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [http://pdbe.org/4gut PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [http://www.ebi.ac.uk/pdbsum/4gut PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gut ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/GLYR1_HUMAN GLYR1_HUMAN]] May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3).<ref>PMID:16352664</ref> <ref>PMID:20850016</ref>	+	[[http://www.uniprot.org/uniprot/KDM1B_HUMAN KDM1B_HUMAN]] Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4 (By similarity). [[http://www.uniprot.org/uniprot/GLYR1_HUMAN GLYR1_HUMAN]] May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3).<ref>PMID:16352664</ref> <ref>PMID:20850016</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4gut" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Lysine-specific histone demethylase 1\|Lysine-specific histone demethylase 1]]	+	*[[Lysine-specific histone demethylase\|Lysine-specific histone demethylase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Chen, F]]		[[Category: Chen, F]]
	[[Category: Dong, Z]]		[[Category: Dong, Z]]

OCA at 20:48, 25 December 2014

OCA — Thu, 25 Dec 2014 20:48:26 GMT

←Older revision		Revision as of 20:48, 25 December 2014
Line 8:		Line 8:
	<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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [http://www.ebi.ac.uk/pdbsum/4gut 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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [http://www.ebi.ac.uk/pdbsum/4gut PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GLYR1_HUMAN GLYR1_HUMAN]] May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3).<ref>PMID:16352664</ref> <ref>PMID:20850016</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:42, 21 December 2014

OCA — Sun, 21 Dec 2014 11:42:24 GMT

←Older revision		Revision as of 11:42, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4gut\| PDB~~=4gut \| ~~SCENE~~= }}	+	==Crystal structure of LSD2-NPAC==
-	===~~Crystal~~ structure of LSD2-~~NPAC~~===	+	<StructureSection load='4gut' size='340' side='right' caption='[[4gut]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23260659}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gut]] 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=4GUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GUT FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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">[[4gu1\|4gu1]], [[4gur\|4gur]], [[4gus\|4gus]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LSD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), GLYR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4gut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gut RCSB], [http://www.ebi.ac.uk/pdbsum/4gut PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Dynamic regulation of histone methylation represents a fundamental epigenetic mechanism underlying eukaryotic gene regulation, yet little is known about how the catalytic activities of histone demethylases are regulated. Here, we identify and characterize NPAC/GLYR1 as an LSD2/KDM1b-specific cofactor that stimulates H3K4me1 and H3K4me2 demethylation. We determine the crystal structures of LSD2 alone and LSD2 in complex with the NPAC linker region in the absence or presence of histone H3 peptide, at resolutions of 2.9, 2.0, and 2.25 A, respectively. These crystal structures and further biochemical characterization define a dodecapeptide of NPAC (residues 214-225) as the minimal functional unit for its cofactor activity and provide structural determinants and a molecular mechanism underlying the intrinsic cofactor activity of NPAC in stimulating LSD2-catalyzed H3K4 demethylation. Thus, these findings establish a model for how a cofactor directly regulates histone demethylation and will have a significant impact on our understanding of catalytic-activity-based epigenetic regulation.

-	~~==Function==~~	+	LSD2/KDM1B and Its Cofactor NPAC/GLYR1 Endow a Structural and Molecular Model for Regulation of H3K4 Demethylation.,Fang R, Chen F, Dong Z, Hu D, Barbera AJ, Clark EA, Fang J, Yang Y, Mei P, Rutenberg M, Li Z, Zhang Y, Xu Y, Yang H, Wang P, Simon MD, Zhou Q, Li J, Marynick MP, Li X, Lu H, Kaiser UB, Kingston RE, Xu Y, Shi YG Mol Cell. 2012 Dec 19. pii: S1097-2765(12)00976-8. doi:, 10.1016/j.molcel.2012.11.019. PMID:23260659<ref>PMID:23260659</ref>
-	~~[[http:~~//~~www.uniprot.org/uniprot/GLYR1_HUMAN GLYR1_HUMAN]] May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14~~ and ~~specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation~~ of ~~MAPK14 and activation of ATF2~~. ~~The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin~~, ~~recognizes and binds trimethylated 'Lys~~-~~36' of histone H3~~ (~~H3K36me3~~).~~<ref>PMID~~:~~16352664<~~/~~ref>~~ <ref>PMID:~~20850016~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4gut]] 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=4GUT OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023260659</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Lysine-specific histone demethylase 1\|Lysine-specific histone demethylase 1]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Chen, F.]]	+	[[Category: Chen, F]]
-	[[Category: Dong, Z.]]	+	[[Category: Dong, Z]]
-	[[Category: Fang, J.]]	+	[[Category: Fang, J]]
-	[[Category: Fang, R.]]	+	[[Category: Fang, R]]
-	[[Category: Li, Z.]]	+	[[Category: Li, Z]]
-	[[Category: Shi, Y.]]	+	[[Category: Shi, Y]]
-	[[Category: Wang, P.]]	+	[[Category: Wang, P]]
-	[[Category: Xu, Y.]]	+	[[Category: Xu, Y]]
-	[[Category: Yang, H.]]	+	[[Category: Yang, H]]
-	[[Category: Yang, Y.]]	+	[[Category: Yang, Y]]
	[[Category: Histone demethylase]]		[[Category: Histone demethylase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 14:26, 10 July 2013

OCA — Wed, 10 Jul 2013 14:26:41 GMT

←Older revision		Revision as of 14:26, 10 July 2013
Line 1:		Line 1:
-	[[Image:4gut.jpg\|left\|200px]]
-
	{{STRUCTURE_4gut\| PDB=4gut \| SCENE= }}		{{STRUCTURE_4gut\| PDB=4gut \| SCENE= }}
-
	===Crystal structure of LSD2-NPAC===		===Crystal structure of LSD2-NPAC===
-
	{{ABSTRACT_PUBMED_23260659}}		{{ABSTRACT_PUBMED_23260659}}
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/GLYR1_HUMAN GLYR1_HUMAN]] May have oxidoreductase activity. Regulates p38 MAP kinase activity by mediating stress activation of p38alpha/MAPK14 and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6. Recruited on chromatin, recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3).<ref>PMID:16352664</ref> <ref>PMID:20850016</ref>

	==About this Structure==		==About this Structure==
	[[4gut]] 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=4GUT OCA].		[[4gut]] 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=4GUT OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023260659</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chen, F.]]		[[Category: Chen, F.]]

OCA at 08:55, 16 January 2013

OCA — Wed, 16 Jan 2013 08:55:07 GMT

←Older revision		Revision as of 08:55, 16 January 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gut.jpg\|left\|200px]]

-	~~The entry~~ 4gut ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4gut\| PDB=4gut \| SCENE= }}

-	~~Authors: Chen, F., Dong, Z., Fang, J., Yang, Y., Li, Z., Xu, Y., Yang, H., Wang, P., Fang, R., Shi, Y., Xu, Y.~~	+	===Crystal structure of LSD2-NPAC===

-	~~Description: Crystal~~ structure ~~of LSD2~~-~~NPAC~~	+	{{ABSTRACT_PUBMED_23260659}}
		+
		+	==About this Structure==
		+	[[4gut]] 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=4GUT OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Chen, F.]]
		+	[[Category: Dong, Z.]]
		+	[[Category: Fang, J.]]
		+	[[Category: Fang, R.]]
		+	[[Category: Li, Z.]]
		+	[[Category: Shi, Y.]]
		+	[[Category: Wang, P.]]
		+	[[Category: Xu, Y.]]
		+	[[Category: Yang, H.]]
		+	[[Category: Yang, Y.]]
		+	[[Category: Histone demethylase]]
		+	[[Category: Oxidoreductase]]

OCA at 09:01, 21 November 2012

OCA — Wed, 21 Nov 2012 09:01:58 GMT

←Older revision		Revision as of 09:01, 21 November 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gut is ON HOLD	+	The entry 4gut is ON HOLD until Paper Publication

	Authors: Chen, F., Dong, Z., Fang, J., Yang, Y., Li, Z., Xu, Y., Yang, H., Wang, P., Fang, R., Shi, Y., Xu, Y.		Authors: Chen, F., Dong, Z., Fang, J., Yang, Y., Li, Z., Xu, Y., Yang, H., Wang, P., Fang, R., Shi, Y., Xu, Y.

	Description: Crystal structure of LSD2-NPAC		Description: Crystal structure of LSD2-NPAC

OCA at 04:53, 12 September 2012

OCA — Wed, 12 Sep 2012 04:53:46 GMT

←Older revision		Revision as of 04:53, 12 September 2012
Line 3:		Line 3:
	The entry 4gut is ON HOLD		The entry 4gut is ON HOLD

-	Authors: ~~Fei~~ Chen, ~~Zhenghong~~ Dong, ~~Jian~~ Fang, ~~Ying~~ Yang, Ze Li, ~~Youwei~~ Xu, ~~Huirong~~ Yang, ~~Ping~~ Wang, ~~Rui~~ Fang, ~~Yujiang~~ Shi, ~~Yanhui~~ Xu	+	Authors: Chen, F., Dong, Z., Fang, J., Yang, Y., Li, Z., Xu, Y., Yang, H., Wang, P., Fang, R., Shi, Y., Xu, Y.

-	Description: ~~crystal~~ structure of LSD2-NPAC	+	Description: Crystal structure of LSD2-NPAC

OCA: Protected "4gut" [edit=sysop:move=sysop]

OCA — Wed, 05 Sep 2012 05:00:08 GMT

Protected "4gut" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:00, 5 September 2012