4ly1 - Revision history

OCA at 16:28, 20 September 2023

2023-09-20T16:28:08Z

←Older revision		Revision as of 16:28, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ly1]] is a 3 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=4LY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LY1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ly1]] is a 3 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=4LY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LY1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=20Y:4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE'>20Y</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 1.57Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=20Y:4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE'>20Y</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [https://pdbe.org/4ly1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ly1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ly1 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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [https://pdbe.org/4ly1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ly1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ly1 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:39, 21 December 2022

2022-12-21T10:39:29Z

←Older revision		Revision as of 10:39, 21 December 2022
Line 1:		Line 1:

	==Structure of Human HDAC2 in complex with inhibitor 4-(acetylamino)-N-[2-amino-5-(thiophen-2-yl)phenyl]benzamide==		==Structure of Human HDAC2 in complex with inhibitor 4-(acetylamino)-N-[2-amino-5-(thiophen-2-yl)phenyl]benzamide==
-	<StructureSection load='4ly1' size='340' side='right' caption='[[4ly1]], [[Resolution\|resolution]] 1.57Å' scene=''>	+	<StructureSection load='4ly1' size='340' side='right'caption='[[4ly1]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ly1]] is a 3 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=4LY1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LY1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ly1]] is a 3 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=4LY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LY1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=20Y:4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE'>20Y</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=20Y:4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE'>20Y</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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">[[4lxz\|4lxz]]</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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [https://pdbe.org/4ly1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ly1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ly1 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [~~http~~://pdbe.org/4ly1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ly1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ly1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>	+	[https://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Histone deacetylase\|Histone deacetylase]]	+	*[[Histone deacetylase 3D structures\|Histone deacetylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone deacetylase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Fong, R]]	+	[[Category: Fong R]]
-	[[Category: Lupardus~~, P J]]~~	+	[[Category: Lupardus PJ]]
-	~~[[Category: Deacetylase]]~~	+
-	~~[[Category: Histone]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex~~]]	+

OCA at 13:21, 5 August 2016

2016-08-05T13:21:29Z

←Older revision		Revision as of 13:21, 5 August 2016
Line 1:		Line 1:
		+
	==Structure of Human HDAC2 in complex with inhibitor 4-(acetylamino)-N-[2-amino-5-(thiophen-2-yl)phenyl]benzamide==		==Structure of Human HDAC2 in complex with inhibitor 4-(acetylamino)-N-[2-amino-5-(thiophen-2-yl)phenyl]benzamide==
	<StructureSection load='4ly1' size='340' side='right' caption='[[4ly1]], [[Resolution\|resolution]] 1.57Å' scene=''>		<StructureSection load='4ly1' size='340' side='right' caption='[[4ly1]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ly1]] is a 3 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=4LY1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LY1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ly1]] is a 3 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=4LY1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LY1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=20Y:4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE'>20Y</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=20Y:4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE'>20Y</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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">[[4lxz\|4lxz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lxz\|4lxz]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC2 ([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">HDAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ly1 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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [http://pdbe.org/4ly1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ly1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ly1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4ly1" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Histone deacetylase]]		[[Category: Histone deacetylase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Fong, R]]		[[Category: Fong, R]]
	[[Category: Lupardus, P J]]		[[Category: Lupardus, P J]]

OCA at 02:49, 25 December 2014

2014-12-25T02:49:05Z

←Older revision		Revision as of 02:49, 25 December 2014
Line 9:		Line 9:
	<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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ly1 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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ly1 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 14:41, 21 December 2014

2014-12-21T14:41:11Z

←Older revision		Revision as of 14:41, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ly1\| PDB=4ly1 \| SCENE= }}~~	+	==Structure of Human HDAC2 in complex with inhibitor 4-(acetylamino)-N-[2-amino-5-(thiophen-2-yl)phenyl]benzamide==
-	===Structure of Human HDAC2 in complex with inhibitor 4-(acetylamino)-N-[2-amino-5-(thiophen-2-yl)phenyl]benzamide===	+	<StructureSection load='4ly1' size='340' side='right' caption='[[4ly1]], [[Resolution\|resolution]] 1.57Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23897821}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ly1]] is a 3 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=4LY1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LY1 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=20Y:4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE'>20Y</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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">[[4lxz\|4lxz]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </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=4ly1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ly1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ly1 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Histone deacetylases (HDACs) are critical in the control of gene expression and dysregulation of their activity has been implicated in a broad range of diseases including cancer, cardiovascular and neurological diseases. HDAC inhibitors (HDACi) employing different zinc chelating functionalities such as hydroxamic acids and benzamides have shown promising results in cancer therapy. While it has also been suggested that HDACi with increased isozyme-selectivity and potency may broaden their clinical utility and minimize side effects, the translation of this idea to the clinic remains to be investigated. Moreover, a detailed understanding of how HDACi with different pharmacological properties affect biological functions in vitro and in vivo is still missing. Here we show that a panel of benzamide-containing HDACi are slow tight-binding inhibitors with long residence times unlike the hydroxamate-containing HDACi SAHA and TSA. Characterization of changes in H2BK5 and H4K14 acetylation following HDACi treatment in the neuroblastoma cell line SH-SY5Y revealed that the timing and magnitude of histone acetylation mirrored both the association and dissociation kinetic rates of the inhibitors. In contrast, cell viability and microarray gene expression analysis indicated that cell death induction and changes in transcriptional regulation do not correlate with the dissociation kinetic rates of the HDACi. Therefore, our study suggests that the evaluation of different classes of HDACi compounds using recombinant HDACs or histone acetylation is insufficient to predict their functional impact on cell activity.

-	~~==Function==~~	+	Histone deacetylase (HDAC) inhibitor kinetic rate constants correlate with cellular histone acetylation but not transcription and cell viability.,Lauffer BE, Mintzer R, Fong R, Mukund S, Tam C, Zilberleyb I, Flicke B, Ritscher A, Fedorowicz G, Vallero R, Ortwine DF, Gunzner J, Modrusan Z, Neumann L, Koth CM, Lupardus PJ, Kaminker JS, Heise CE, Steiner P J Biol Chem. 2013 Jul 29. PMID:23897821<ref>PMID:23897821</ref>
-	~~[[http://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones~~ (~~H2A, H2B, H3 and H4~~)~~. Histone deacetylation gives a tag for epigenetic repression~~ and ~~plays an important role in transcriptional regulation,~~ cell ~~cycle progression and developmental events~~. ~~Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD~~, ~~SIN3~~, ~~YY1 and N-COR. Interacts in the late~~ S~~-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1~~, ~~DMAP1~~, ~~PCNA~~, ~~CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses~~, ~~via histone deacetylase (HDAC) recruitment~~, ~~a number of genes implicated in multilineage blood cell development~~.<ref>PMID:~~19343227~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4ly1]] is~~ a ~~3 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=4LY1 OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023897821</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Histone deacetylase\|Histone deacetylase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Histone deacetylase]]		[[Category: Histone deacetylase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Fong, R.]]	+	[[Category: Fong, R]]
-	[[Category: Lupardus, P J.]]	+	[[Category: Lupardus, P J]]
	[[Category: Deacetylase]]		[[Category: Deacetylase]]
	[[Category: Histone]]		[[Category: Histone]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA at 08:21, 21 August 2013

2013-08-21T08:21:31Z

←Older revision		Revision as of 08:21, 21 August 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4ly1\| PDB=4ly1 \| SCENE= }}
		+	===Structure of Human HDAC2 in complex with inhibitor 4-(acetylamino)-N-[2-amino-5-(thiophen-2-yl)phenyl]benzamide===
		+	{{ABSTRACT_PUBMED_23897821}}

-	~~The entry 4ly1 is ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/HDAC2_HUMAN HDAC2_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development.<ref>PMID:19343227</ref>

-	~~Authors~~: ~~Fong, R~~.~~, Lupardus, P~~.J.	+	==About this Structure==
		+	[[4ly1]] is a 3 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=4LY1 OCA].

-	~~Description~~: ~~Structure of Human HDAC2 in complex with~~ inhibitor ~~(Compound 1)~~	+	==Reference==
		+	<ref group="xtra">PMID:023897821</ref><references group="xtra"/><references/>
		+	[[Category: Histone deacetylase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Fong, R.]]
		+	[[Category: Lupardus, P J.]]
		+	[[Category: Deacetylase]]
		+	[[Category: Histone]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]

OCA: Protected "4ly1" [edit=sysop:move=sysop]

2013-08-07T20:20:53Z

Protected "4ly1" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:20, 7 August 2013

OCA: New page: '''Unreleased structure''' The entry 4ly1 is ON HOLD Authors: Fong, R., Lupardus, P.J. Description: Structure of Human HDAC2 in complex with inhibitor (Compound 1)

2013-08-07T20:20:52Z

New page: '''Unreleased structure''' The entry 4ly1 is ON HOLD Authors: Fong, R., Lupardus, P.J. Description: Structure of Human HDAC2 in complex with inhibitor (Compound 1)

New page

'''Unreleased structure'''

The entry 4ly1 is ON HOLD

Authors: Fong, R., Lupardus, P.J.

Description: Structure of Human HDAC2 in complex with inhibitor (Compound 1)