5b77 - Revision history

OCA at 16:02, 8 November 2023

2023-11-08T16:02:46Z

←Older revision		Revision as of 16:02, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5b77]] 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=5B77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B77 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5b77]] 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=5B77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B77 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.551Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5b77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b77 OCA], [https://pdbe.org/5b77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b77 RCSB], [https://www.ebi.ac.uk/pdbsum/5b77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b77 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=5b77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b77 OCA], [https://pdbe.org/5b77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b77 RCSB], [https://www.ebi.ac.uk/pdbsum/5b77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b77 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:40, 31 May 2023

2023-05-31T06:40:53Z

←Older revision		Revision as of 06:40, 31 May 2023
Line 3:		Line 3:
	<StructureSection load='5b77' size='340' side='right'caption='[[5b77]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='5b77' size='340' side='right'caption='[[5b77]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5b77]] 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=5B77 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5B77 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5b77]] 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=5B77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B77 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</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=5b77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b77 OCA], [https://pdbe.org/5b77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b77 RCSB], [https://www.ebi.ac.uk/pdbsum/5b77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b77 ProSAT]</span></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td><~~td class="sblockDat">MOZ ([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_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48]~~ </~~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=5b77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b77 OCA], [~~http~~://pdbe.org/5b77 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5b77 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5b77 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5b77 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Note=Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP; translocation t(8;22)(p11;q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation. Note=A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein.	+	[https://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN] Note=Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP; translocation t(8;22)(p11;q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation. Note=A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2.<ref>PMID:11742995</ref> <ref>PMID:11965546</ref> <ref>PMID:12771199</ref> <ref>PMID:16387653</ref> <ref>PMID:17925393</ref>	+	[https://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN] Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2.<ref>PMID:11742995</ref> <ref>PMID:11965546</ref> <ref>PMID:12771199</ref> <ref>PMID:16387653</ref> <ref>PMID:17925393</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone acetyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Li, H]]	+	[[Category: Li H]]
-	[[Category: Xiong, X]]	+	[[Category: Xiong X]]
-	~~[[Category: Moz double phd finger]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:48, 11 March 2020

2020-03-11T08:48:06Z

←Older revision		Revision as of 08:48, 11 March 2020
Line 1:		Line 1:

	==Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at K14==		==Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at K14==
-	<StructureSection load='5b77' size='340' side='right' caption='[[5b77]], [[Resolution\|resolution]] 1.55Å' scene=''>	+	<StructureSection load='5b77' size='340' side='right'caption='[[5b77]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5b77]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B77 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5b77]] 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=5B77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B77 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=SO4:SULFATE+ION'>SO4</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=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MOZ ([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_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=5b77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b77 OCA], [http://pdbe.org/5b77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b77 RCSB], [http://www.ebi.ac.uk/pdbsum/5b77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b77 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=5b77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b77 OCA], [http://pdbe.org/5b77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b77 RCSB], [http://www.ebi.ac.uk/pdbsum/5b77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b77 ProSAT]</span></td></tr>
Line 22:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 5b77" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5b77" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone acetyltransferase 3D structures\|Histone acetyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Histone acetyltransferase]]		[[Category: Histone acetyltransferase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Li, H]]		[[Category: Li, H]]
	[[Category: Xiong, X]]		[[Category: Xiong, X]]
	[[Category: Moz double phd finger]]		[[Category: Moz double phd finger]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 18:42, 10 December 2016

2016-12-10T18:42:34Z

←Older revision		Revision as of 18:42, 10 December 2016
Line 13:		Line 13:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2.<ref>PMID:11742995</ref> <ref>PMID:11965546</ref> <ref>PMID:12771199</ref> <ref>PMID:16387653</ref> <ref>PMID:17925393</ref>		[[http://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2.<ref>PMID:11742995</ref> <ref>PMID:11965546</ref> <ref>PMID:12771199</ref> <ref>PMID:16387653</ref> <ref>PMID:17925393</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Recognition of histone covalent modifications by 'reader' modules constitutes a major mechanism for epigenetic regulation. A recent upsurge of newly discovered histone lysine acylations, such as crotonylation (Kcr), butyrylation (Kbu), and propionylation (Kpr), greatly expands the coding potential of histone lysine modifications. Here we demonstrate that the histone acetylation-binding double PHD finger (DPF) domains of human MOZ (also known as KAT6A) and DPF2 (also known as BAF45d) accommodate a wide range of histone lysine acylations with the strongest preference for Kcr. Crystal structures of the DPF domain of MOZ in complex with H3K14cr, H3K14bu, and H3K14pr peptides reveal that these non-acetyl acylations are anchored in a hydrophobic 'dead-end' pocket with selectivity for crotonylation arising from intimate encapsulation and an amide-sensing hydrogen bonding network. Immunofluorescence and chromatin immunoprecipitation (ChIP)-quantitative PCR (qPCR) showed that MOZ and H3K14cr colocalize in a DPF-dependent manner. Our studies call attention to a new regulatory mechanism centered on histone crotonylation readout by DPF family members.
		+
		+	Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2.,Xiong X, Panchenko T, Yang S, Zhao S, Yan P, Zhang W, Xie W, Li Y, Zhao Y, Allis CD, Li H Nat Chem Biol. 2016 Dec;12(12):1111-1118. doi: 10.1038/nchembio.2218. Epub 2016, Oct 24. PMID:27775714<ref>PMID:27775714</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5b77" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:38, 26 October 2016

2016-10-26T18:38:25Z

←Older revision		Revision as of 18:38, 26 October 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5b77 is ~~ON HOLD~~	+	==Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at K14==
-		+	<StructureSection load='5b77' size='340' side='right' caption='[[5b77]], [[Resolution\|resolution]] 1.55Å' scene=''>
-	~~Authors~~: Li, H., ~~Xiong~~, X.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5b77]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B77 FirstGlance]. <br>
-	~~Description~~: ~~Crystal structrue~~ of ~~MOZ double PHD finger~~ in ~~complex~~ with histone H3 ~~propionylation at K14~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</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_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </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=5b77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b77 OCA], [http://pdbe.org/5b77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b77 RCSB], [http://www.ebi.ac.uk/pdbsum/5b77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b77 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Note=Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP; translocation t(8;22)(p11;q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation. Note=A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KAT6A_HUMAN KAT6A_HUMAN]] Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2.<ref>PMID:11742995</ref> <ref>PMID:11965546</ref> <ref>PMID:12771199</ref> <ref>PMID:16387653</ref> <ref>PMID:17925393</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone acetyltransferase]]
	[[Category: Li, H]]		[[Category: Li, H]]
	[[Category: Xiong, X]]		[[Category: Xiong, X]]
		+	[[Category: Moz double phd finger]]
		+	[[Category: Transferase]]

OCA at 16:47, 23 June 2016

2016-06-23T16:47:04Z

←Older revision		Revision as of 16:47, 23 June 2016
Line 3:		Line 3:
	The entry 5b77 is ON HOLD		The entry 5b77 is ON HOLD

-	Authors: Li, ~~Haitao~~, ~~Xiaozhe~~ Xiong	+	Authors: Li, H., Xiong, X.

	Description: Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at K14		Description: Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at K14
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Li, ~~Haitao, Xiaozhe~~ Xiong]]	+	[[Category: Li, H]]
		+	[[Category: Xiong, X]]

OCA: Protected "5b77" [edit=sysop:move=sysop]

2016-06-20T09:05:28Z

Protected "5b77" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:05, 20 June 2016

OCA: New page: '''Unreleased structure''' The entry 5b77 is ON HOLD Authors: Li, Haitao, Xiaozhe Xiong Description: Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylatio...

2016-06-20T09:05:27Z

New page: '''Unreleased structure''' The entry 5b77 is ON HOLD Authors: Li, Haitao, Xiaozhe Xiong Description: Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylatio...

New page

'''Unreleased structure'''

The entry 5b77 is ON HOLD

Authors: Li, Haitao, Xiaozhe Xiong

Description: Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at K14
[[Category: Unreleased Structures]]
[[Category: Li, Haitao, Xiaozhe Xiong]]