5vi6 - Revision history

OCA at 13:49, 4 October 2023

OCA — Wed, 04 Oct 2023 13:49:09 GMT

←Older revision		Revision as of 13:49, 4 October 2023
Line 3:		Line 3:
	<StructureSection load='5vi6' size='340' side='right'caption='[[5vi6]], [[Resolution\|resolution]] 1.24Å' scene=''>		<StructureSection load='5vi6' size='340' side='right'caption='[[5vi6]], [[Resolution\|resolution]] 1.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5vi6]] 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=5VI6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5VI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5vi6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicoma_ambiens Helicoma ambiens] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VI6 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=DIO:1,4~~-~~DIETHYLENE+DIOXIDE'>DIO</scene>~~, ~~<scene name='pdbligand=EDO:~~1~~,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 1.237Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=5OM:(2S)-2-AMINO-8,8-DIHYDROXY-8-[(2S)-OXIRAN-2-YL]OCTANOIC+ACID'>5OM</scene>, <scene name='pdbligand=CPI:6-CARBOXYPIPERIDINE'>CPI</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5OM:(2S)-2-AMINO-8,8-DIHYDROXY-8-[(2S)-OXIRAN-2-YL]OCTANOIC+ACID'>5OM</scene>, <scene name='pdbligand=CPI:6-CARBOXYPIPERIDINE'>CPI</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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">HDAC8~~, ~~HDACL1, CDA07 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5vi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi6 OCA], [https://pdbe.org/5vi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vi6 RCSB], [https://www.ebi.ac.uk/pdbsum/5vi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi6 ProSAT]</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=5vi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi6 OCA], [~~http~~://pdbe.org/5vi6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5vi6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5vi6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>	+	[https://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</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: ~~Histone deacetylase~~]]	+	[[Category: Helicoma ambiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Christianson~~, D W~~]]	+	[[Category: Christianson DW]]
-	[[Category: Porter~~, N J]]~~	+	[[Category: Porter NJ]]
-	~~[[Category: Epigenetic]]~~	+
-	~~[[Category: Hdac]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Natural product inhibitor~~]]	+

OCA at 09:34, 1 January 2020

OCA — Wed, 01 Jan 2020 09:34:00 GMT

←Older revision		Revision as of 09:34, 1 January 2020
Line 1:		Line 1:

	==Crystal structure of histone deacetylase 8 in complex with trapoxin A==		==Crystal structure of histone deacetylase 8 in complex with trapoxin A==
-	<StructureSection load='5vi6' size='340' side='right' caption='[[5vi6]], [[Resolution\|resolution]] 1.24Å' scene=''>	+	<StructureSection load='5vi6' size='340' side='right'caption='[[5vi6]], [[Resolution\|resolution]] 1.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5vi6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5vi6]] 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=5VI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VI6 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5OM:(2S)-2-AMINO-8,8-DIHYDROXY-8-[(2S)-OXIRAN-2-YL]OCTANOIC+ACID'>5OM</scene>, <scene name='pdbligand=CPI:6-CARBOXYPIPERIDINE'>CPI</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5OM:(2S)-2-AMINO-8,8-DIHYDROXY-8-[(2S)-OXIRAN-2-YL]OCTANOIC+ACID'>5OM</scene>, <scene name='pdbligand=CPI:6-CARBOXYPIPERIDINE'>CPI</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HDAC8, HDACL1, CDA07 ([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=5vi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi6 OCA], [http://pdbe.org/5vi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi6 ProSAT]</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=5vi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi6 OCA], [http://pdbe.org/5vi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi6 ProSAT]</span></td></tr>
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5vi6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5vi6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone deacetylase 3D structures\|Histone deacetylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Histone deacetylase]]		[[Category: Histone deacetylase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]
	[[Category: Porter, N J]]		[[Category: Porter, N J]]

OCA at 09:50, 13 September 2017

OCA — Wed, 13 Sep 2017 09:50:43 GMT

←Older revision		Revision as of 09:50, 13 September 2017
Line 3:		Line 3:
	<StructureSection load='5vi6' size='340' side='right' caption='[[5vi6]], [[Resolution\|resolution]] 1.24Å' scene=''>		<StructureSection load='5vi6' size='340' side='right' caption='[[5vi6]], [[Resolution\|resolution]] 1.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5vi6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5vi6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VI6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=~~TXG~~:(~~3S,6S,9S,15aR~~)-~~6,9~~-~~dibenzyl~~-~~3-{6~~,6-~~dihydroxy~~-6-[(2S)-~~oxiran~~-2-yl]~~hexyl}octahydro-2H-pyrido[1,2-a][1,4,7,10]tetraazacyclododecine-1,4,7,10(3H,12H)-tetrone~~'>~~TXG~~</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=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5OM:(2S)-2-AMINO-8,8-DIHYDROXY-8-[(2S)-OXIRAN-2-YL]OCTANOIC+ACID'>5OM</scene>, <scene name='pdbligand=CPI:6-CARBOXYPIPERIDINE'>CPI</scene></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=5vi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi6 OCA], [http://pdbe.org/5vi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi6 ProSAT]</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=5vi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi6 OCA], [http://pdbe.org/5vi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi6 ProSAT]</span></td></tr>
Line 29:		Line 30:
	[[Category: Hdac]]		[[Category: Hdac]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
	[[Category: Natural product inhibitor]]		[[Category: Natural product inhibitor]]

OCA at 03:46, 6 September 2017

OCA — Wed, 06 Sep 2017 03:46:44 GMT

←Older revision		Revision as of 03:46, 6 September 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5vi6 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of histone deacetylase 8 in complex with trapoxin A==
		+	<StructureSection load='5vi6' size='340' side='right' caption='[[5vi6]], [[Resolution\|resolution]] 1.24Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5vi6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VI6 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TXG:(3S,6S,9S,15aR)-6,9-dibenzyl-3-{6,6-dihydroxy-6-[(2S)-oxiran-2-yl]hexyl}octahydro-2H-pyrido[1,2-a][1,4,7,10]tetraazacyclododecine-1,4,7,10(3H,12H)-tetrone'>TXG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5vi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi6 OCA], [http://pdbe.org/5vi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi6 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Trapoxin A is a microbial cyclic tetrapeptide that is an essentially irreversible inhibitor of class I histone deacetylases (HDACs). The inhibitory warhead is the alpha,beta-epoxyketone side-chain of (2S,9S)-2-amino-8-oxo-9,10-epoxydecanoic acid (l-Aoe), which mimics the side-chain of the HDAC substrate acetyl-l-lysine. We now report the crystal structure of the HDAC8-trapoxin A complex at 1.24 A resolution, revealing that the ketone moiety of l-Aoe undergoes nucleophilic attack to form a zinc-bound tetrahedral gem-diolate that mimics the tetrahedral intermediate and its flanking transition states in catalysis. Mass spectrometry, activity measurements, and isothermal titration calorimetry confirm that trapoxin A binds tightly (Kd = 3 +/- 1 nM) and does not covalently modify the enzyme, so the epoxide moiety of l-Aoe remains intact. Comparison of the HDAC8-trapoxin A complex with the HDAC6-HC toxin complex provides new insight regarding the inhibitory potency of l-Aoe-containing natural products against class I and class II HDACs.

-	~~Authors:~~ Porter, N.J.~~, Christianson, D~~.W.	+	Binding of the Microbial Cyclic Tetrapeptide Trapoxin A to the Class I Histone Deacetylase HDAC8.,Porter NJ, Christianson DW ACS Chem Biol. 2017 Aug 30. doi: 10.1021/acschembio.7b00330. PMID:28846375<ref>PMID:28846375</ref>

-	~~Description: Crystal structure~~ of ~~histone~~ deacetylase ~~8 in complex with trapoxin A~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: Porter, N.J]]	+	<div class="pdbe-citations 5vi6" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Christianson, D.W~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone deacetylase]]
		+	[[Category: Christianson, D W]]
		+	[[Category: Porter, N J]]
		+	[[Category: Epigenetic]]
		+	[[Category: Hdac]]
		+	[[Category: Hydrolase]]
		+	[[Category: Natural product inhibitor]]

OCA at 11:32, 24 May 2017

OCA — Wed, 24 May 2017 11:32:46 GMT

←Older revision		Revision as of 11:32, 24 May 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5vi6 is ON HOLD	+	The entry 5vi6 is ON HOLD until Paper Publication

	Authors: Porter, N.J., Christianson, D.W.		Authors: Porter, N.J., Christianson, D.W.

OCA: Protected "5vi6" [edit=sysop:move=sysop]

OCA — Thu, 27 Apr 2017 12:18:40 GMT

Protected "5vi6" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:18, 27 April 2017

OCA: New page: '''Unreleased structure''' The entry 5vi6 is ON HOLD Authors: Porter, N.J., Christianson, D.W. Description: Crystal structure of histone deacetylase 8 in complex with trapoxin A [[Cate...

OCA — Thu, 27 Apr 2017 12:18:39 GMT

New page: '''Unreleased structure''' The entry 5vi6 is ON HOLD Authors: Porter, N.J., Christianson, D.W. Description: Crystal structure of histone deacetylase 8 in complex with trapoxin A [[Cate...

New page

'''Unreleased structure'''

The entry 5vi6 is ON HOLD

Authors: Porter, N.J., Christianson, D.W.

Description: Crystal structure of histone deacetylase 8 in complex with trapoxin A
[[Category: Unreleased Structures]]
[[Category: Porter, N.J]]
[[Category: Christianson, D.W]]