5tab - Revision history

OCA at 14:20, 6 March 2024

2024-03-06T14:20:11Z

← Older revision		Revision as of 14:20, 6 March 2024
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	<StructureSection load='5tab' size='340' side='right'caption='[[5tab]], [[Resolution\|resolution]] 1.25Å' scene=''>		<StructureSection load='5tab' size='340' side='right'caption='[[5tab]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tab]] is a 1 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=5TAB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tab]] is a 1 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=5TAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TAB FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=GOL:GLYCEROL'>GOL</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]] 1.25Å</td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~PHF20, C20orf104, GLEA2, HCA58, NZF, TZP ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN])~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5tab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tab OCA], [~~http~~://pdbe.org/5tab PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tab RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tab PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tab 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=5tab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tab OCA], [https://pdbe.org/5tab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tab RCSB], [https://www.ebi.ac.uk/pdbsum/5tab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tab ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/PHF20_HUMAN PHF20_HUMAN]] Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage.<ref>PMID:20018852</ref> <ref>PMID:22864287</ref>		[https://www.uniprot.org/uniprot/PHF20_HUMAN PHF20_HUMAN] Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage.<ref>PMID:20018852</ref> <ref>PMID:22864287</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	PHF20 is a core component of the lysine acetyltransferase complex MOF (male absent on the first)-NSL (non-specific lethal) that generates the major epigenetic mark H4K16ac and is necessary for transcriptional regulation and DNA repair. The role of PHF20 in the complex remains elusive. Here, we report on functional coupling between methylation readers in PHF20. We show that the plant homeodomain (PHD) finger of PHF20 recognizes dimethylated lysine 4 of histone H3 (H3K4me2) and represents an example of a native reader that selects for this modification. Biochemical and structural analyses help to explain this selectivity and the preference of Tudor2, another reader in PHF20, for dimethylated p53. Binding of the PHD finger to H3K4me2 is required for histone acetylation, accumulation of PHF20 at target genes, and transcriptional activation. Together, our findings establish a unique PHF20-mediated link between MOF histone acetyltransferase (HAT), p53, and H3K4me2, and suggest a model for rapid spreading of H4K16ac-enriched open chromatin.

	PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation.,Klein BJ, Wang X, Cui G, Yuan C, Botuyan MV, Lin K, Lu Y, Wang X, Zhao Y, Bruns CJ, Mer G, Shi X, Kutateladze TG Cell Rep. 2016 Oct 18;17(4):1158-1170. doi: 10.1016/j.celrep.2016.09.056. PMID:27760318<ref>PMID:27760318</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 5tab" style="background-color:#fffaf0;"></div~~>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Klein~~, B J~~]]		[[Category: Klein BJ]]
	[[Category: Kutateladze~~, T G]]~~		[[Category: Kutateladze TG]]
	~~[[Category: Phd finger]]~~
	~~[[Category: Transcription~~]]

OCA at 12:29, 25 December 2019

2019-12-25T12:29:57Z

← Older revision		Revision as of 12:29, 25 December 2019
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	==Crystal Structure of the PHD Finger of PHF20==		==Crystal Structure of the PHD Finger of PHF20==
	<StructureSection load='5tab' size='340' side='right' caption='[[5tab]], [[Resolution\|resolution]] 1.25Å' scene=''>		<StructureSection load='5tab' size='340' side='right'caption='[[5tab]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tab]] is a 1 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=5TAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tab]] is a 1 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=5TAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TAB FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Klein, B J]]		[[Category: Klein, B J]]
	[[Category: Kutateladze, T G]]		[[Category: Kutateladze, T G]]
	[[Category: Phd finger]]		[[Category: Phd finger]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 05:51, 16 May 2018

2018-05-16T05:51:42Z

← Older revision		Revision as of 05:51, 16 May 2018
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PHF20_HUMAN PHF20_HUMAN]] Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage.<ref>PMID:20018852</ref> <ref>PMID:22864287</ref>		[[http://www.uniprot.org/uniprot/PHF20_HUMAN PHF20_HUMAN]] Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage.<ref>PMID:20018852</ref> <ref>PMID:22864287</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			PHF20 is a core component of the lysine acetyltransferase complex MOF (male absent on the first)-NSL (non-specific lethal) that generates the major epigenetic mark H4K16ac and is necessary for transcriptional regulation and DNA repair. The role of PHF20 in the complex remains elusive. Here, we report on functional coupling between methylation readers in PHF20. We show that the plant homeodomain (PHD) finger of PHF20 recognizes dimethylated lysine 4 of histone H3 (H3K4me2) and represents an example of a native reader that selects for this modification. Biochemical and structural analyses help to explain this selectivity and the preference of Tudor2, another reader in PHF20, for dimethylated p53. Binding of the PHD finger to H3K4me2 is required for histone acetylation, accumulation of PHF20 at target genes, and transcriptional activation. Together, our findings establish a unique PHF20-mediated link between MOF histone acetyltransferase (HAT), p53, and H3K4me2, and suggest a model for rapid spreading of H4K16ac-enriched open chromatin.

			PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation.,Klein BJ, Wang X, Cui G, Yuan C, Botuyan MV, Lin K, Lu Y, Wang X, Zhao Y, Bruns CJ, Mer G, Shi X, Kutateladze TG Cell Rep. 2016 Oct 18;17(4):1158-1170. doi: 10.1016/j.celrep.2016.09.056. PMID:27760318<ref>PMID:27760318</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 5tab" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:01, 15 November 2017

2017-11-15T19:01:18Z

← Older revision		Revision as of 19:01, 15 November 2017
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	<StructureSection load='5tab' size='340' side='right' caption='[[5tab]], [[Resolution\|resolution]] 1.25Å' scene=''>		<StructureSection load='5tab' size='340' side='right' caption='[[5tab]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tab]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tab]] is a 1 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=5TAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TAB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=GOL:GLYCEROL'>GOL</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">PHF20, C20orf104, GLEA2, HCA58, NZF, TZP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tab OCA], [http://pdbe.org/5tab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tab RCSB], [http://www.ebi.ac.uk/pdbsum/5tab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tab 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=5tab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tab OCA], [http://pdbe.org/5tab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tab RCSB], [http://www.ebi.ac.uk/pdbsum/5tab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tab ProSAT]</span></td></tr>
	</table>		</table>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
	[[Category: Klein, B J]]		[[Category: Klein, B J]]
	[[Category: Kutateladze, T G]]		[[Category: Kutateladze, T G]]
	[[Category: Phd finger]]		[[Category: Phd finger]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 18:51, 26 October 2016

2016-10-26T18:51:19Z

← Older revision		Revision as of 18:51, 26 October 2016
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 5tab is ~~ON HOLD~~		==Crystal Structure of the PHD Finger of PHF20==
			<StructureSection load='5tab' size='340' side='right' caption='[[5tab]], [[Resolution\|resolution]] 1.25Å' scene=''>
	~~Authors~~:		== Structural highlights ==
			<table><tr><td colspan='2'>[[5tab]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TAB FirstGlance]. <br>
	~~Description~~:		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	[[Category: ~~Unreleased Structures~~]]		<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=5tab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tab OCA], [http://pdbe.org/5tab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tab RCSB], [http://www.ebi.ac.uk/pdbsum/5tab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tab ProSAT]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/PHF20_HUMAN PHF20_HUMAN]] Methyllysine-binding protein, component of the MOF histone acetyltransferase protein complex. Not required for maintaining the global histone H4 'Lys-16' acetylation (H4K16ac) levels or locus specific histone acetylation, but instead works downstream in transcriptional regulation of MOF target genes (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Contributes to methyllysine-dependent p53/TP53 stabilization and up-regulation after DNA damage.<ref>PMID:20018852</ref> <ref>PMID:22864287</ref>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Klein, B J]]
			[[Category: Kutateladze, T G]]
			[[Category: Phd finger]]
			[[Category: Transcription]]

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

2016-09-21T12:25:14Z

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

← Older revision	Revision as of 12:25, 21 September 2016
(No difference)

OCA: New page: '''Unreleased structure''' The entry 5tab is ON HOLD Authors: Description: Category: Unreleased Structures

2016-09-21T12:25:12Z

New page: '''Unreleased structure''' The entry 5tab is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5tab is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]