5xfn - Revision history

OCA at 10:18, 27 March 2024

OCA — Wed, 27 Mar 2024 10:18:17 GMT

←Older revision		Revision as of 10:18, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='5xfn' size='340' side='right'caption='[[5xfn]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='5xfn' size='340' side='right'caption='[[5xfn]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xfn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5XFN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xfn]] 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=5XFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XFN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<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]] 1.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5xfo\|5xfo]], [[5xfp\|5xfp]], [[5xfq\|5xfq]], [[5xfr\|5xfr]]~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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~~://proteopedia.org/fgij/fg.htm?mol=5xfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfn OCA], [~~http~~://pdbe.org/5xfn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5xfn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5xfn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfn 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=5xfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfn OCA], [https://pdbe.org/5xfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xfn RCSB], [https://www.ebi.ac.uk/pdbsum/5xfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PHF1_HUMAN PHF1_HUMAN]] Transcriptional repressor. May promote methylation of histone H3 on 'Lys-27' by the PRC2/EED-EZH2 complex.<ref>PMID:18086877</ref> <ref>PMID:18285464</ref>	+	[https://www.uniprot.org/uniprot/PHF1_HUMAN PHF1_HUMAN] Transcriptional repressor. May promote methylation of histone H3 on 'Lys-27' by the PRC2/EED-EZH2 complex.<ref>PMID:18086877</ref> <ref>PMID:18285464</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The Polycomb repressive complex 2 (PRC2) mainly mediates transcriptional repression and has essential roles in various biological processes including the maintenance of cell identity and proper differentiation. Polycomb-like (PCL) proteins, such as PHF1, MTF2 and PHF19, are PRC2-associated factors that form sub-complexes with PRC2 core components, and have been proposed to modulate the enzymatic activity of PRC2 or the recruitment of PRC2 to specific genomic loci. Mammalian PRC2-binding sites are enriched in CG content, which correlates with CpG islands that display a low level of DNA methylation. However, the mechanism of PRC2 recruitment to CpG islands is not fully understood. Here we solve the crystal structures of the N-terminal domains of PHF1 and MTF2 with bound CpG-containing DNAs in the presence of H3K36me3-containing histone peptides. We show that the extended homologous regions of both proteins fold into a winged-helix structure, which specifically binds to the unmethylated CpG motif but in a completely different manner from the canonical winged-helix DNA recognition motif. We also show that the PCL extended homologous domains are required for efficient recruitment of PRC2 to CpG island-containing promoters in mouse embryonic stem cells. Our research provides the first, to our knowledge, direct evidence to demonstrate that PCL proteins are crucial for PRC2 recruitment to CpG islands, and further clarifies the roles of these proteins in transcriptional regulation in vivo.	+
-		+
-	Polycomb-like proteins link the PRC2 complex to CpG islands.,Li H, Liefke R, Jiang J, Kurland JV, Tian W, Deng P, Zhang W, He Q, Patel DJ, Bulyk ML, Shi Y, Wang Z Nature. 2017 Sep 14;549(7671):287-291. doi: 10.1038/nature23881. Epub 2017 Sep 6. PMID:28869966<ref>PMID:28869966</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5xfn" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Li, H]]	+	[[Category: Li H]]
-	[[Category: Wang, Z]]	+	[[Category: Wang Z]]
-	~~[[Category: Pcl1]]~~	+
-	~~[[Category: Phf1]]~~	+
-	~~[[Category: Prc2]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 06:48, 14 October 2020

OCA — Wed, 14 Oct 2020 06:48:34 GMT

←Older revision		Revision as of 06:48, 14 October 2020
Line 1:		Line 1:

	==Structure of the N-terminal domains of PHF1==		==Structure of the N-terminal domains of PHF1==
-	<StructureSection load='5xfn' size='340' side='right' caption='[[5xfn]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='5xfn' size='340' side='right'caption='[[5xfn]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xfn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFN OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XFN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xfn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XFN 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=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5xfo\|5xfo]], [[5xfp\|5xfp]], [[5xfq\|5xfq]], [[5xfr\|5xfr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5xfo\|5xfo]], [[5xfp\|5xfp]], [[5xfq\|5xfq]], [[5xfr\|5xfr]]</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=5xfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfn OCA], [http://pdbe.org/5xfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xfn RCSB], [http://www.ebi.ac.uk/pdbsum/5xfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfn ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfn OCA], [http://pdbe.org/5xfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xfn RCSB], [http://www.ebi.ac.uk/pdbsum/5xfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Li, H]]		[[Category: Li, H]]
	[[Category: Wang, Z]]		[[Category: Wang, Z]]

OCA at 09:32, 27 September 2017

OCA — Wed, 27 Sep 2017 09:32:31 GMT

←Older revision		Revision as of 09:32, 27 September 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5xfn is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Structure of the N-terminal domains of PHF1==
		+	<StructureSection load='5xfn' size='340' side='right' caption='[[5xfn]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5xfn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XFN 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>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5xfo\|5xfo]], [[5xfp\|5xfp]], [[5xfq\|5xfq]], [[5xfr\|5xfr]]</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=5xfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfn OCA], [http://pdbe.org/5xfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xfn RCSB], [http://www.ebi.ac.uk/pdbsum/5xfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfn ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PHF1_HUMAN PHF1_HUMAN]] Transcriptional repressor. May promote methylation of histone H3 on 'Lys-27' by the PRC2/EED-EZH2 complex.<ref>PMID:18086877</ref> <ref>PMID:18285464</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Polycomb repressive complex 2 (PRC2) mainly mediates transcriptional repression and has essential roles in various biological processes including the maintenance of cell identity and proper differentiation. Polycomb-like (PCL) proteins, such as PHF1, MTF2 and PHF19, are PRC2-associated factors that form sub-complexes with PRC2 core components, and have been proposed to modulate the enzymatic activity of PRC2 or the recruitment of PRC2 to specific genomic loci. Mammalian PRC2-binding sites are enriched in CG content, which correlates with CpG islands that display a low level of DNA methylation. However, the mechanism of PRC2 recruitment to CpG islands is not fully understood. Here we solve the crystal structures of the N-terminal domains of PHF1 and MTF2 with bound CpG-containing DNAs in the presence of H3K36me3-containing histone peptides. We show that the extended homologous regions of both proteins fold into a winged-helix structure, which specifically binds to the unmethylated CpG motif but in a completely different manner from the canonical winged-helix DNA recognition motif. We also show that the PCL extended homologous domains are required for efficient recruitment of PRC2 to CpG island-containing promoters in mouse embryonic stem cells. Our research provides the first, to our knowledge, direct evidence to demonstrate that PCL proteins are crucial for PRC2 recruitment to CpG islands, and further clarifies the roles of these proteins in transcriptional regulation in vivo.

-	~~Authors~~:	+	Polycomb-like proteins link the PRC2 complex to CpG islands.,Li H, Liefke R, Jiang J, Kurland JV, Tian W, Deng P, Zhang W, He Q, Patel DJ, Bulyk ML, Shi Y, Wang Z Nature. 2017 Sep 14;549(7671):287-291. doi: 10.1038/nature23881. Epub 2017 Sep 6. PMID:28869966<ref>PMID:28869966</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5xfn" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Li, H]]
		+	[[Category: Wang, Z]]
		+	[[Category: Pcl1]]
		+	[[Category: Phf1]]
		+	[[Category: Prc2]]
		+	[[Category: Transcription]]

OCA at 12:08, 4 May 2017

OCA — Thu, 04 May 2017 12:08:52 GMT

←Older revision		Revision as of 12:08, 4 May 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 19 Apr 2017 12:08:35 GMT

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

←Older revision

Revision as of 12:08, 19 April 2017

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

OCA — Wed, 19 Apr 2017 12:08:34 GMT

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

New page

'''Unreleased structure'''

The entry 5xfn is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]