4llb - Revision history

OCA at 16:20, 20 September 2023

2023-09-20T16:20:51Z

←Older revision		Revision as of 16:20, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4llb]] is a 4 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=4LLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LLB FirstGlance]. <br>		<table><tr><td colspan='2'>[[4llb]] is a 4 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=4LLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LLB FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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]] 2.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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=4llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llb OCA], [https://pdbe.org/4llb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4llb RCSB], [https://www.ebi.ac.uk/pdbsum/4llb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4llb 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=4llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llb OCA], [https://pdbe.org/4llb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4llb RCSB], [https://www.ebi.ac.uk/pdbsum/4llb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4llb ProSAT]</span></td></tr>
	</table>		</table>

OCA at 11:08, 14 December 2022

2022-12-14T11:08:25Z

←Older revision		Revision as of 11:08, 14 December 2022
Line 1:		Line 1:

	==Crystal Structure of MOZ double PHD finger histone H3K14ac complex==		==Crystal Structure of MOZ double PHD finger histone H3K14ac complex==
-	<StructureSection load='4llb' size='340' side='right' caption='[[4llb]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4llb' size='340' side='right'caption='[[4llb]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4llb]] is a 4 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=4LLB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LLB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4llb]] is a 4 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=4LLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LLB FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"~~><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=ALY:N(6)-ACETYLLYSINE'>ALY</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=ALY:N(6)-ACETYLLYSINE'>ALY</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=4llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llb OCA], [https://pdbe.org/4llb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4llb RCSB], [https://www.ebi.ac.uk/pdbsum/4llb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4llb ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lka\|4lka]]~~, ~~[[4lk9\|4lk9]], [[4ljn\|4ljn]]~~<~~/td></tr>~~	+
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">KAT6A, MOZ, MYST3, RUNXBP2, ZNF220 ([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=4llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llb OCA], [~~http~~://pdbe.org/4llb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4llb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4llb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4llb 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 26:		Line 22:

	==See Also==		==See Also==
-	*[[Histone acetyltransferase\|Histone acetyltransferase]]	+	*[[Histone acetyltransferase 3D structures\|Histone acetyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone acetyltransferase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Deeves~~, S E~~]]	+	[[Category: Deeves SE]]
-	[[Category: Dreveny, I]]	+	[[Category: Dreveny I]]
-	[[Category: Heery~~, D M~~]]	+	[[Category: Heery DM]]
-	[[Category: Yue, B]]	+	[[Category: Yue B]]
-	~~[[Category: Double phd finger]]~~	+
-	~~[[Category: Dpf]]~~	+
-	~~[[Category: Dpf - h3k14ac complex]]~~	+
-	~~[[Category: Histone h3 tail]]~~	+
-	~~[[Category: Plant homeodomain]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Zinc finger~~]]	+

OCA at 15:28, 4 August 2016

2016-08-04T15:28:38Z

←Older revision		Revision as of 15:28, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of MOZ double PHD finger histone H3K14ac complex==		==Crystal Structure of MOZ double PHD finger histone H3K14ac complex==
	<StructureSection load='4llb' size='340' side='right' caption='[[4llb]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4llb' size='340' side='right' caption='[[4llb]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 8:		Line 9:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KAT6A, MOZ, MYST3, RUNXBP2, ZNF220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KAT6A, MOZ, MYST3, RUNXBP2, ZNF220 ([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=4llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4llb RCSB], [http://www.ebi.ac.uk/pdbsum/4llb 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=4llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llb OCA], [http://pdbe.org/4llb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4llb RCSB], [http://www.ebi.ac.uk/pdbsum/4llb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4llb ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 22:		Line 23:
	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 4llb" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone acetyltransferase\|Histone acetyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:32, 21 December 2014

2014-12-21T17:32:19Z

←Older revision		Revision as of 17:32, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4llb\| PDB=4llb \| SCENE= }}~~	+	==Crystal Structure of MOZ double PHD finger histone H3K14ac complex==
-	===Crystal Structure of MOZ double PHD finger histone H3K14ac complex===	+	<StructureSection load='4llb' size='340' side='right' caption='[[4llb]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24150941}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4llb]] is a 4 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=4LLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LLB FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4lka\|4lka]], [[4lk9\|4lk9]], [[4ljn\|4ljn]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KAT6A, MOZ, MYST3, RUNXBP2, ZNF220 ([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=4llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4llb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4llb RCSB], [http://www.ebi.ac.uk/pdbsum/4llb PDBsum]</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.		[[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 ==
-	==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 ==
		+	Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYST3/KAT6A. In addition to sampling H3 and H4 modification status, we show that the DPF cooperates with the MYST domain to promote H3K9 and H3K14 acetylation, although not if H3K4 is trimethylated. Four crystal structures of an extended DPF alone and in complex with unmodified or acetylated forms of the H3 tail reveal the molecular basis of crosstalk between H3K4me3 and H3K14ac. We show for the first time that MOZ DPF induces alpha-helical conformation of H3K4-T11, revealing a unique mode of H3 recognition. The helical structure facilitates sampling of H3K4 methylation status, and proffers H3K9 and other residues for modification. Additionally, we show that a conserved double glycine hinge flanking the H3 tail helix is required for a conformational change enabling docking of H3K14ac with the DPF. In summary, our data provide the first observations of extensive helical structure in a histone tail, revealing the inherent ability of the H3 tail to adopt alternate conformations in complex with chromatin regulators.

-	~~==About this Structure==~~	+	The double PHD finger domain of MOZ/MYST3 induces alpha-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.,Dreveny I, Deeves SE, Fulton J, Yue B, Messmer M, Bhattacharya A, Collins HM, Heery DM Nucleic Acids Res. 2014 Jan 1;42(2):822-35. doi: 10.1093/nar/gkt931. Epub 2013, Oct 22. PMID:24150941<ref>PMID:24150941</ref>
-	~~[[4llb]] is a 4 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=4LLB OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024150941</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Histone acetyltransferase]]		[[Category: Histone acetyltransferase]]
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Deeves, S E.]]	+	[[Category: Deeves, S E]]
-	[[Category: Dreveny, I.]]	+	[[Category: Dreveny, I]]
-	[[Category: Heery, D M.]]	+	[[Category: Heery, D M]]
-	[[Category: Yue, B.]]	+	[[Category: Yue, B]]
	[[Category: Double phd finger]]		[[Category: Double phd finger]]
	[[Category: Dpf]]		[[Category: Dpf]]
	[[Category: Dpf - h3k14ac complex]]		[[Category: Dpf - h3k14ac complex]]
-	[[Category: Histone acetyltransferase]]
	[[Category: Histone h3 tail]]		[[Category: Histone h3 tail]]
	[[Category: Plant homeodomain]]		[[Category: Plant homeodomain]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Zinc finger]]		[[Category: Zinc finger]]

OCA at 09:13, 5 February 2014

2014-02-05T09:13:32Z

←Older revision		Revision as of 09:13, 5 February 2014
Line 1:		Line 1:
	{{STRUCTURE_4llb\| PDB=4llb \| SCENE= }}		{{STRUCTURE_4llb\| PDB=4llb \| SCENE= }}
	===Crystal Structure of MOZ double PHD finger histone H3K14ac complex===		===Crystal Structure of MOZ double PHD finger histone H3K14ac complex===
		+	{{ABSTRACT_PUBMED_24150941}}

	==Disease==		==Disease==
Line 9:		Line 10:

	==About this Structure==		==About this Structure==
-	[[4llb]] is a 4 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=4LLB OCA].	+	[[4llb]] is a 4 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=4LLB OCA].

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024150941</ref><references group="xtra"/><references/>
	[[Category: Histone acetyltransferase]]		[[Category: Histone acetyltransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Deeves, S E.]]		[[Category: Deeves, S E.]]
	[[Category: Dreveny, I.]]		[[Category: Dreveny, I.]]

OCA at 08:09, 16 October 2013

2013-10-16T08:09:50Z

←Older revision		Revision as of 08:09, 16 October 2013
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-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4llb\| PDB=4llb \| SCENE= }}
		+	===Crystal Structure of MOZ double PHD finger histone H3K14ac complex===

-	~~The entry 4llb is ON HOLD~~ ~~until Paper Publication~~	+	==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.

-	~~Authors~~: ~~Dreveny, I~~.~~, Deeves, S~~.E.~~, Yue, B~~.~~, Heery, D.M~~.	+	==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>

-	~~Description: Crystal~~ Structure ~~of MOZ double PHD~~ finger ~~histone H3K14ac~~ complex	+	==About this Structure==
		+	[[4llb]] is a 4 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=4LLB OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Histone acetyltransferase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Deeves, S E.]]
		+	[[Category: Dreveny, I.]]
		+	[[Category: Heery, D M.]]
		+	[[Category: Yue, B.]]
		+	[[Category: Double phd finger]]
		+	[[Category: Dpf]]
		+	[[Category: Dpf - h3k14ac complex]]
		+	[[Category: Histone acetyltransferase]]
		+	[[Category: Histone h3 tail]]
		+	[[Category: Plant homeodomain]]
		+	[[Category: Transferase]]
		+	[[Category: Zinc finger]]

OCA at 06:44, 28 August 2013

2013-08-28T06:44:42Z

←Older revision		Revision as of 06:44, 28 August 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Dreveny, I., Deeves, S.E., Yue, B., Heery, D.M.		Authors: Dreveny, I., Deeves, S.E., Yue, B., Heery, D.M.

	Description: Crystal Structure of MOZ double PHD finger histone H3K14ac complex		Description: Crystal Structure of MOZ double PHD finger histone H3K14ac complex

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

2013-07-18T04:47:44Z

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

←Older revision

Revision as of 04:47, 18 July 2013

OCA: New page: '''Unreleased structure''' The entry 4llb is ON HOLD Authors: Dreveny, I., Deeves, S.E., Yue, B., Heery, D.M. Description: Crystal Structure of MOZ double PHD finger histone H3K14ac co...

2013-07-18T04:47:43Z

New page: '''Unreleased structure''' The entry 4llb is ON HOLD Authors: Dreveny, I., Deeves, S.E., Yue, B., Heery, D.M. Description: Crystal Structure of MOZ double PHD finger histone H3K14ac co...

New page

'''Unreleased structure'''

The entry 4llb is ON HOLD

Authors: Dreveny, I., Deeves, S.E., Yue, B., Heery, D.M.

Description: Crystal Structure of MOZ double PHD finger histone H3K14ac complex