4c5i - Revision history

OCA at 12:04, 20 December 2023

OCA — Wed, 20 Dec 2023 12:04:16 GMT

←Older revision		Revision as of 12:04, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5I FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5I FirstGlance]. <br>
-	</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=4c5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5i OCA], [https://pdbe.org/4c5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5i RCSB], [https://www.ebi.ac.uk/pdbsum/4c5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5i ProSAT]</span></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]] 2.586Å</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=4c5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5i OCA], [https://pdbe.org/4c5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5i RCSB], [https://www.ebi.ac.uk/pdbsum/4c5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MBTD1_HUMAN MBTD1_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4.	+	[https://www.uniprot.org/uniprot/MBTD1_HUMAN MBTD1_HUMAN] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Polycomb group (PcG) protein complexes repress developmental regulator genes by modifying their chromatin. How different PcG proteins assemble into complexes and are recruited to their target genes is poorly understood. Here, we report the crystal structure of the core of the Drosophila PcG protein complex Pleiohomeotic (Pho)-repressive complex (PhoRC), which contains the Polycomb response element (PRE)-binding protein Pho and Sfmbt. The spacer region of Pho, separated from the DNA-binding domain by a long flexible linker, forms a tight complex with the four malignant brain tumor (4MBT) domain of Sfmbt. The highly conserved spacer region of the human Pho ortholog YY1 binds three of the four human 4MBT domain proteins in an analogous manner but with lower affinity. Comparison of the Drosophila Pho:Sfmbt and human YY1:MBTD1 complex structures provides a molecular explanation for the lower affinity of YY1 for human 4MBT domain proteins. Structure-guided mutations that disrupt the interaction between Pho and Sfmbt abolish formation of a ternary Sfmbt:Pho:DNA complex in vitro and repression of developmental regulator genes in Drosophila. PRE tethering of Sfmbt by Pho is therefore essential for Polycomb repression in Drosophila. Our results support a model where DNA tethering of Sfmbt by Pho and multivalent interactions of Sfmbt with histone modifications and other PcG proteins create a hub for PcG protein complex assembly at PREs.
		+
		+	Structural basis for targeting the chromatin repressor Sfmbt to Polycomb response elements.,Alfieri C, Gambetta MC, Matos R, Glatt S, Sehr P, Fraterman S, Wilm M, Muller J, Muller CW Genes Dev. 2013 Nov 1;27(21):2367-79. doi: 10.1101/gad.226621.113. PMID:24186981<ref>PMID:24186981</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c5i" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:27, 7 September 2022

OCA — Wed, 07 Sep 2022 17:27:58 GMT

←Older revision		Revision as of 17:27, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c5i' size='340' side='right'caption='[[4c5i]], [[Resolution\|resolution]] 2.59Å' scene=''>		<StructureSection load='4c5i' size='340' side='right'caption='[[4c5i]], [[Resolution\|resolution]] 2.59Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C5I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5I FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5e\|4c5e]], [[4c5g\|4c5g]], [[4c5h\|4c5h]]</td></tr>~~	+	</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=4c5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5i OCA], [https://pdbe.org/4c5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5i RCSB], [https://www.ebi.ac.uk/pdbsum/4c5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5i 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=4c5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5i OCA], [~~http~~://pdbe.org/4c5i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c5i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c5i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5i ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MBTD1_HUMAN MBTD1_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. [[http://www.uniprot.org/uniprot/TYY1_HUMAN TYY1_HUMAN]] Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions).<ref>PMID:17721549</ref> <ref>PMID:18026119</ref> Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements.<ref>PMID:17721549</ref> <ref>PMID:18026119</ref>	+	[[https://www.uniprot.org/uniprot/MBTD1_HUMAN MBTD1_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Polycomb group (PcG) protein complexes repress developmental regulator genes by modifying their chromatin. How different PcG proteins assemble into complexes and are recruited to their target genes is poorly understood. Here, we report the crystal structure of the core of the Drosophila PcG protein complex Pleiohomeotic (Pho)-repressive complex (PhoRC), which contains the Polycomb response element (PRE)-binding protein Pho and Sfmbt. The spacer region of Pho, separated from the DNA-binding domain by a long flexible linker, forms a tight complex with the four malignant brain tumor (4MBT) domain of Sfmbt. The highly conserved spacer region of the human Pho ortholog YY1 binds three of the four human 4MBT domain proteins in an analogous manner but with lower affinity. Comparison of the Drosophila Pho:Sfmbt and human YY1:MBTD1 complex structures provides a molecular explanation for the lower affinity of YY1 for human 4MBT domain proteins. Structure-guided mutations that disrupt the interaction between Pho and Sfmbt abolish formation of a ternary Sfmbt:Pho:DNA complex in vitro and repression of developmental regulator genes in Drosophila. PRE tethering of Sfmbt by Pho is therefore essential for Polycomb repression in Drosophila. Our results support a model where DNA tethering of Sfmbt by Pho and multivalent interactions of Sfmbt with histone modifications and other PcG proteins create a hub for PcG protein complex assembly at PREs.	+
-		+
-	Structural basis for targeting the chromatin repressor Sfmbt to Polycomb response elements.,Alfieri C, Gambetta MC, Matos R, Glatt S, Sehr P, Fraterman S, Wilm M, Muller J, Muller CW Genes Dev. 2013 Nov 1;27(21):2367-79. doi: 10.1101/gad.226621.113. PMID:24186981<ref>PMID:24186981</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c5i" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Alfieri, C]]	+	[[Category: Alfieri C]]
-	[[Category: Glatt, S]]	+	[[Category: Glatt S]]
-	[[Category: Mueller~~, C W]]~~	+	[[Category: Mueller CW]]
-	~~[[Category: Transcription~~]]	+

OCA at 09:32, 20 March 2019

OCA — Wed, 20 Mar 2019 09:32:27 GMT

←Older revision		Revision as of 09:32, 20 March 2019
Line 1:		Line 1:

	==Crystal structure of MBTD1 YY1 complex==		==Crystal structure of MBTD1 YY1 complex==
-	<StructureSection load='4c5i' size='340' side='right' caption='[[4c5i]], [[Resolution\|resolution]] 2.59Å' scene=''>	+	<StructureSection load='4c5i' size='340' side='right'caption='[[4c5i]], [[Resolution\|resolution]] 2.59Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5I FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5I FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Alfieri, C]]		[[Category: Alfieri, C]]
	[[Category: Glatt, S]]		[[Category: Glatt, S]]
	[[Category: Mueller, C W]]		[[Category: Mueller, C W]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 07:26, 5 August 2016

OCA — Fri, 05 Aug 2016 07:26:12 GMT

←Older revision		Revision as of 07:26, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of MBTD1 YY1 complex==		==Crystal structure of MBTD1 YY1 complex==
	<StructureSection load='4c5i' size='340' side='right' caption='[[4c5i]], [[Resolution\|resolution]] 2.59Å' scene=''>		<StructureSection load='4c5i' size='340' side='right' caption='[[4c5i]], [[Resolution\|resolution]] 2.59Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5I FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5I FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5e\|4c5e]], [[4c5g\|4c5g]], [[4c5h\|4c5h]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5e\|4c5e]], [[4c5g\|4c5g]], [[4c5h\|4c5h]]</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=4c5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c5i RCSB], [http://www.ebi.ac.uk/pdbsum/4c5i 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=4c5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5i OCA], [http://pdbe.org/4c5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c5i RCSB], [http://www.ebi.ac.uk/pdbsum/4c5i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4c5i" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:52, 25 December 2014

OCA — Thu, 25 Dec 2014 16:52:16 GMT

←Older revision		Revision as of 16:52, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c5i\| PDB~~=4c5i \| ~~SCENE~~= }}	+	==Crystal structure of MBTD1 YY1 complex==
-	===~~Crystal~~ structure ~~of MBTD1 YY1 complex~~===	+	<StructureSection load='4c5i' size='340' side='right' caption='[[4c5i]], [[Resolution\|resolution]] 2.59Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24186981}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4c5i]] is a 3 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=4C5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5I FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c5e\|4c5e]], [[4c5g\|4c5g]], [[4c5h\|4c5h]]</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=4c5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c5i RCSB], [http://www.ebi.ac.uk/pdbsum/4c5i PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/MBTD1_HUMAN MBTD1_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. [[http://www.uniprot.org/uniprot/TYY1_HUMAN TYY1_HUMAN]] Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions).<ref>PMID:17721549</ref> <ref>PMID:18026119</ref> Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements.<ref>PMID:17721549</ref> <ref>PMID:18026119</ref>		[[http://www.uniprot.org/uniprot/MBTD1_HUMAN MBTD1_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. [[http://www.uniprot.org/uniprot/TYY1_HUMAN TYY1_HUMAN]] Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions).<ref>PMID:17721549</ref> <ref>PMID:18026119</ref> Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements.<ref>PMID:17721549</ref> <ref>PMID:18026119</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Polycomb group (PcG) protein complexes repress developmental regulator genes by modifying their chromatin. How different PcG proteins assemble into complexes and are recruited to their target genes is poorly understood. Here, we report the crystal structure of the core of the Drosophila PcG protein complex Pleiohomeotic (Pho)-repressive complex (PhoRC), which contains the Polycomb response element (PRE)-binding protein Pho and Sfmbt. The spacer region of Pho, separated from the DNA-binding domain by a long flexible linker, forms a tight complex with the four malignant brain tumor (4MBT) domain of Sfmbt. The highly conserved spacer region of the human Pho ortholog YY1 binds three of the four human 4MBT domain proteins in an analogous manner but with lower affinity. Comparison of the Drosophila Pho:Sfmbt and human YY1:MBTD1 complex structures provides a molecular explanation for the lower affinity of YY1 for human 4MBT domain proteins. Structure-guided mutations that disrupt the interaction between Pho and Sfmbt abolish formation of a ternary Sfmbt:Pho:DNA complex in vitro and repression of developmental regulator genes in Drosophila. PRE tethering of Sfmbt by Pho is therefore essential for Polycomb repression in Drosophila. Our results support a model where DNA tethering of Sfmbt by Pho and multivalent interactions of Sfmbt with histone modifications and other PcG proteins create a hub for PcG protein complex assembly at PREs.

-	~~==About this Structure==~~	+	Structural basis for targeting the chromatin repressor Sfmbt to Polycomb response elements.,Alfieri C, Gambetta MC, Matos R, Glatt S, Sehr P, Fraterman S, Wilm M, Muller J, Muller CW Genes Dev. 2013 Nov 1;27(21):2367-79. doi: 10.1101/gad.226621.113. PMID:24186981<ref>PMID:24186981</ref>
-	~~[[4c5i]] is a 3 chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=4C5I OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024186981</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Alfieri, C.]]	+	== References ==
-	[[Category: Glatt, S.]]	+	<references/>
-	[[Category: Mueller, C W.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Alfieri, C]]
		+	[[Category: Glatt, S]]
		+	[[Category: Mueller, C W]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 08:18, 13 November 2013

OCA — Wed, 13 Nov 2013 08:18:10 GMT

←Older revision		Revision as of 08:18, 13 November 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4c5i\| PDB=4c5i \| SCENE= }}
		+	===Crystal structure of MBTD1 YY1 complex===
		+	{{ABSTRACT_PUBMED_24186981}}

-	The ~~entry 4c5i~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/MBTD1_HUMAN MBTD1_HUMAN]] Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility (By similarity). Specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. [[http://www.uniprot.org/uniprot/TYY1_HUMAN TYY1_HUMAN]] Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions).<ref>PMID:17721549</ref> <ref>PMID:18026119</ref> Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements.<ref>PMID:17721549</ref> <ref>PMID:18026119</ref>

-	~~Authors~~: ~~Alfieri, C~~.~~, Glatt, S~~.~~, Mueller, C~~.W.	+	==About this Structure==
		+	[[4c5i]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5I OCA].

-	~~Description~~: ~~Crystal structure of MBTD1 YY1 complex~~	+	==Reference==
		+	<ref group="xtra">PMID:024186981</ref><references group="xtra"/><references/>
		+	[[Category: Alfieri, C.]]
		+	[[Category: Glatt, S.]]
		+	[[Category: Mueller, C W.]]
		+	[[Category: Transcription]]

OCA at 06:32, 2 October 2013

OCA — Wed, 02 Oct 2013 06:32:15 GMT

←Older revision		Revision as of 06:32, 2 October 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c5i is ON HOLD	+	The entry 4c5i is ON HOLD until Paper Publication

-	Authors: Alfieri, C., Glatt, S.	+	Authors: Alfieri, C., Glatt, S., Mueller, C.W.

	Description: Crystal structure of MBTD1 YY1 complex		Description: Crystal structure of MBTD1 YY1 complex

OCA: Protected "4c5i" [edit=sysop:move=sysop]

OCA — Fri, 20 Sep 2013 03:19:03 GMT

Protected "4c5i" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:19, 20 September 2013

OCA: New page: '''Unreleased structure''' The entry 4c5i is ON HOLD Authors: Alfieri, C., Glatt, S. Description: Crystal structure of MBTD1 YY1 complex

OCA — Fri, 20 Sep 2013 03:19:02 GMT

New page: '''Unreleased structure''' The entry 4c5i is ON HOLD Authors: Alfieri, C., Glatt, S. Description: Crystal structure of MBTD1 YY1 complex

New page

'''Unreleased structure'''

The entry 4c5i is ON HOLD

Authors: Alfieri, C., Glatt, S.

Description: Crystal structure of MBTD1 YY1 complex