3oq5 - Revision history

OCA at 09:43, 6 September 2023

OCA — Wed, 06 Sep 2023 09:43:12 GMT

←Older revision		Revision as of 09:43, 6 September 2023
Line 1:		Line 1:

	==Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1==		==Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1==
-	<StructureSection load='3oq5' size='340' side='right' caption='[[3oq5]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='3oq5' size='340' side='right'caption='[[3oq5]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oq5]] is a 5 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=3OQ5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3OQ5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oq5]] is a 5 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=3OQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OQ5 FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=MLZ:N~~-~~METHYL-LYSINE'>MLZ</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]] 2.5005Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~L3MBTL, KIAA0681, L3MBT, L3MBTL1 ([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=MLZ:N-METHYL-LYSINE'>MLZ</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=3oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oq5 OCA], [~~http~~://pdbe.org/3oq5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3oq5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3oq5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3oq5 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=3oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oq5 OCA], [https://pdbe.org/3oq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oq5 RCSB], [https://www.ebi.ac.uk/pdbsum/3oq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oq5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/LMBL1_HUMAN LMBL1_HUMAN]] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.<ref>PMID:17540172</ref> <ref>PMID:18408754</ref> <ref>PMID:20870719</ref> <ref>PMID:20870725</ref> [[http://www.uniprot.org/uniprot/Q5U0E4_HUMAN Q5U0E4_HUMAN]] Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (By similarity).[RuleBase:RU003304]	+	[https://www.uniprot.org/uniprot/LMBL1_HUMAN LMBL1_HUMAN] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.<ref>PMID:17540172</ref> <ref>PMID:18408754</ref> <ref>PMID:20870719</ref> <ref>PMID:20870725</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/3oq5_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/3oq5_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Appella, E]]	+	[[Category: Large Structures]]
-	[[Category: Gozani, O]]	+	[[Category: Appella E]]
-	[[Category: Hayashi, R]]	+	[[Category: Gozani O]]
-	[[Category: Kutateladze, T]]	+	[[Category: Hayashi R]]
-	[[Category: Roy, S]]	+	[[Category: Kutateladze T]]
-	[[Category: Shi, X]]	+	[[Category: Roy S]]
-	[[Category: Weiner~~, K L~~]]	+	[[Category: Shi X]]
-	[[Category: West~~, L E]]~~	+	[[Category: Weiner KL]]
-	~~[[Category: Chromatin regulator]]~~	+	[[Category: West LE]]
-	~~[[Category: Chromosomal protein]]~~	+
-	~~[[Category: Dna-binding]]~~	+
-	~~[[Category: Malignant brain tumor]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Methylation]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: P53]]~~	+
-	~~[[Category: Protein lysine methyltransferase]]~~	+
-	~~[[Category: Repressor]]~~	+
-	~~[[Category: Three-leaved beta-propeller]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transcription regulation]]~~	+
-	~~[[Category: Zinc-finger~~]]	+

OCA at 13:29, 4 August 2016

OCA — Thu, 04 Aug 2016 13:29:19 GMT

←Older revision		Revision as of 13:29, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1==		==Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1==
	<StructureSection load='3oq5' size='340' side='right' caption='[[3oq5]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3oq5' size='340' side='right' caption='[[3oq5]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3oq5]] is a 5 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=3OQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OQ5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3oq5]] is a 5 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=3OQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OQ5 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">L3MBTL, KIAA0681, L3MBT, L3MBTL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">L3MBTL, KIAA0681, L3MBT, L3MBTL1 ([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=3oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oq5 RCSB], [http://www.ebi.ac.uk/pdbsum/3oq5 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=3oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oq5 OCA], [http://pdbe.org/3oq5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oq5 RCSB], [http://www.ebi.ac.uk/pdbsum/3oq5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oq5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3oq5 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	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 3oq5" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Appella, E]]		[[Category: Appella, E]]
	[[Category: Gozani, O]]		[[Category: Gozani, O]]

OCA at 09:43, 25 December 2014

OCA — Thu, 25 Dec 2014 09:43:44 GMT

←Older revision		Revision as of 09:43, 25 December 2014
Line 7:		Line 7:
	<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=3oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oq5 RCSB], [http://www.ebi.ac.uk/pdbsum/3oq5 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=3oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oq5 RCSB], [http://www.ebi.ac.uk/pdbsum/3oq5 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LMBL1_HUMAN LMBL1_HUMAN]] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.<ref>PMID:17540172</ref> <ref>PMID:18408754</ref> <ref>PMID:20870719</ref> <ref>PMID:20870725</ref> [[http://www.uniprot.org/uniprot/Q5U0E4_HUMAN Q5U0E4_HUMAN]] Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (By similarity).[RuleBase:RU003304]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:34, 19 December 2014

OCA — Fri, 19 Dec 2014 06:34:40 GMT

←Older revision		Revision as of 06:34, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3oq5\| PDB=3oq5 \| SCENE= }}~~	+	==Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1==
-	===Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1===	+	<StructureSection load='3oq5' size='340' side='right' caption='[[3oq5]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20870725}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3oq5]] is a 5 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=3OQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OQ5 FirstGlance]. <br>
		+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">L3MBTL, KIAA0681, L3MBT, L3MBTL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3oq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oq5 RCSB], [http://www.ebi.ac.uk/pdbsum/3oq5 PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/3oq5_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The p53 tumor suppressor protein is regulated by multiple post-translational modifications, including lysine methylation. We previously found that monomethylation of p53 at lysine 382 (p53K382me1) by the protein lysine methyltransferase (PKMT) SET8/PR-Set7 represses p53 transactivation of target genes. However, the molecular mechanism linking p53K382 monomethylation to repression is not known. Here we show in biochemical and crystallographic studies the preferential recognition of p53K382me1 by the triple malignant brain tumor (MBT)-repeats of the chromatin compaction factor L3MBTL1. We demonstrate that SET8-mediated methylation of p53 at K382 promotes the interaction between L3MBTL1 and p53 in cells, and the chromatin occupancy of L3MBTL1 at p53 target promoters. In the absence of DNA damage, L3MBTL1 interacts with p53K382me1 and p53-target genes are repressed, whereas depletion of L3MBTL1 results in a p53-dependent increase in p21 and PUMA transcript levels. Activation of p53 by DNA damage is coupled to a decrease in p53K382me1 levels, abrogation of the L3MBTL1-p53 interaction, and disassociation of L3MBTL1 from p53-target promoters. Together, we identify L3MBTL1 as the second known methyl-p53 effector protein, and provide a molecular explanation for the mechanism by which p53K382me1 is transduced to regulate p53 activity.

-	~~==Function==~~	+	The MBT repeats of L3MBTL1 link set8 mediated p53 methylation at lysine 382 to target gene repression.,West LE, Roy S, Lachmi-Weiner K, Hayashi R, Shi X, Appella E, Kutateladze TG, Gozani O J Biol Chem. 2010 Sep 24. PMID:20870725<ref>PMID:20870725</ref>
-	[[http://www.uniprot.org/uniprot/LMBL1_HUMAN LMBL1_HUMAN]] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53~~/TP53 monomethylated~~ at ~~'Lys-~~382~~', leading~~ to ~~repress p53/TP53-~~target ~~genes~~. ~~Also recognizes and binds RB1/RB monomethylated at 'Lys~~-~~860'~~. ~~Participates in the ETV6-mediated repression~~. ~~Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.<ref>~~PMID:~~17540172</ref><ref>PMID:18408754</ref><ref>PMID:20870719</ref>~~<ref>PMID:20870725</ref> [[http://www.uniprot.org/uniprot/Q5U0E4_HUMAN Q5U0E4_HUMAN]] Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (By similarity).[RuleBase:RU003304]	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3oq5]] is~~ a ~~5 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=3OQ5 OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020870725</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Appella, E.]]	+	[[Category: Appella, E]]
-	[[Category: Gozani, O.]]	+	[[Category: Gozani, O]]
-	[[Category: Hayashi, R.]]	+	[[Category: Hayashi, R]]
-	[[Category: Kutateladze, T.]]	+	[[Category: Kutateladze, T]]
-	[[Category: Roy, S.]]	+	[[Category: Roy, S]]
-	[[Category: Shi, X.]]	+	[[Category: Shi, X]]
-	[[Category: Weiner, K L.]]	+	[[Category: Weiner, K L]]
-	[[Category: West, L E.]]	+	[[Category: West, L E]]
	[[Category: Chromatin regulator]]		[[Category: Chromatin regulator]]
	[[Category: Chromosomal protein]]		[[Category: Chromosomal protein]]

OCA: Protected "3oq5" [edit=sysop:move=sysop]

OCA — Sun, 24 Mar 2013 19:25:30 GMT

Protected "3oq5" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:25, 24 March 2013

OCA at 19:25, 24 March 2013

OCA — Sun, 24 Mar 2013 19:25:25 GMT

←Older revision		Revision as of 19:25, 24 March 2013
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-	{{Seed}}
-	[[Image:3oq5.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3oq5", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3oq5\| PDB=3oq5 \| SCENE= }}		{{STRUCTURE_3oq5\| PDB=3oq5 \| SCENE= }}
-
	===Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1===		===Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1===
		+	{{ABSTRACT_PUBMED_20870725}}

-		+	==Function==
-	<!--	+	[[http://www.uniprot.org/uniprot/LMBL1_HUMAN LMBL1_HUMAN]] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.<ref>PMID:17540172</ref><ref>PMID:18408754</ref><ref>PMID:20870719</ref><ref>PMID:20870725</ref> [[http://www.uniprot.org/uniprot/Q5U0E4_HUMAN Q5U0E4_HUMAN]] Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (By similarity).[RuleBase:RU003304]
-	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_20870725}}~~, ~~adds the Publication Abstract~~ to the ~~page~~	+
-	~~(as~~ it ~~appears on PubMed at~~ http://www.~~pubmed~~.~~gov), where 20870725 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20870725}}~~	+

	==About this Structure==		==About this Structure==
-	~~3OQ5~~ is a 5 ~~chains~~ structure with ~~sequences~~ 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=3OQ5 OCA].	+	[[3oq5]] is a 5 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=3OQ5 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20870725~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020870725</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Appella, E.]]		[[Category: Appella, E.]]
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	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]
	[[Category: Zinc-finger]]		[[Category: Zinc-finger]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 13 10:17:18 2010''

OCA at 07:07, 13 October 2010

OCA — Wed, 13 Oct 2010 07:07:30 GMT

←Older revision		Revision as of 07:07, 13 October 2010
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	{{Seed}}		{{Seed}}
-	[[Image:3oq5.~~jpg~~\|left\|200px]]	+	[[Image:3oq5.png\|left\|200px]]

	<!--		<!--
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	===Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1===		===Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20870725}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20870725 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20870725}}

	==About this Structure==		==About this Structure==
	3OQ5 is a 5 chains structure with sequences 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=3OQ5 OCA].		3OQ5 is a 5 chains structure with sequences 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=3OQ5 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20870725</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Appella, E.]]		[[Category: Appella, E.]]
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	[[Category: Zinc-finger]]		[[Category: Zinc-finger]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Sep 22 14~~:50:20 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 13 10:17:18 2010''

OCA at 11:41, 22 September 2010

OCA — Wed, 22 Sep 2010 11:41:21 GMT

←Older revision		Revision as of 11:41, 22 September 2010
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-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3oq5.jpg\|left\|200px]]

-	The ~~entry 3oq5~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3oq5", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3oq5\| PDB=3oq5 \| SCENE= }}

-	~~Authors: Roy, S., West, L.E., Weiner, K.L., Hayashi, R., Shi, X., Appella, E., Gozani, O., Kutateladze, T.~~	+	===Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1===

-	Description: Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep ~~15 10~~:38:37 2010''	+	==About this Structure==
		+	3OQ5 is a 5 chains structure with sequences 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=3OQ5 OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Appella, E.]]
		+	[[Category: Gozani, O.]]
		+	[[Category: Hayashi, R.]]
		+	[[Category: Kutateladze, T.]]
		+	[[Category: Roy, S.]]
		+	[[Category: Shi, X.]]
		+	[[Category: Weiner, K L.]]
		+	[[Category: West, L E.]]
		+	[[Category: Chromatin regulator]]
		+	[[Category: Chromosomal protein]]
		+	[[Category: Dna-binding]]
		+	[[Category: Malignant brain tumor]]
		+	[[Category: Metal-binding]]
		+	[[Category: Methylation]]
		+	[[Category: Nucleus]]
		+	[[Category: P53]]
		+	[[Category: Protein lysine methyltransferase]]
		+	[[Category: Repressor]]
		+	[[Category: Three-leaved beta-propeller]]
		+	[[Category: Transcription]]
		+	[[Category: Transcription regulation]]
		+	[[Category: Zinc-finger]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:50:20 2010''

OCA: New page: '''Unreleased structure''' The entry 3oq5 is ON HOLD Authors: Roy, S., West, L.E., Weiner, K.L., Hayashi, R., Shi, X., Appella, E., Gozani, O., Kutateladze, T. Description: Crystal str...

OCA — Wed, 15 Sep 2010 07:29:54 GMT

New page: '''Unreleased structure''' The entry 3oq5 is ON HOLD Authors: Roy, S., West, L.E., Weiner, K.L., Hayashi, R., Shi, X., Appella, E., Gozani, O., Kutateladze, T. Description: Crystal str...

New page

'''Unreleased structure'''

The entry 3oq5 is ON HOLD

Authors: Roy, S., West, L.E., Weiner, K.L., Hayashi, R., Shi, X., Appella, E., Gozani, O., Kutateladze, T.

Description: Crystal structure of the 3-MBT domain from human L3MBTL1 in complex with p53K382me1

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 15 10:38:37 2010''