4hga - Revision history

OCA at 08:51, 20 March 2024

OCA — Wed, 20 Mar 2024 08:51:54 GMT

←Older revision		Revision as of 08:51, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hga]] 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=4HGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGA FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hga]] 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=4HGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</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]] 2.799Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</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=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [https://pdbe.org/4hga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [https://www.ebi.ac.uk/pdbsum/4hga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hga 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=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [https://pdbe.org/4hga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [https://www.ebi.ac.uk/pdbsum/4hga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hga ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DAXX_HUMAN DAXX_HUMAN] Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.<ref>PMID:12140263</ref> <ref>PMID:15364927</ref> <ref>PMID:17081986</ref> <ref>PMID:16845383</ref>		[https://www.uniprot.org/uniprot/DAXX_HUMAN DAXX_HUMAN] Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.<ref>PMID:12140263</ref> <ref>PMID:15364927</ref> <ref>PMID:17081986</ref> <ref>PMID:16845383</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Mammalian histone H3.3 is a variant of the canonical H3.1 essential for genome reprogramming in fertilized eggs and maintenance of chromatin structure in neuronal cells. An H3.3-specific histone chaperone, DAXX, directs the deposition of H3.3 onto pericentric and telomeric heterochromatin. H3.3 differs from H3.1 by only five amino acids, yet DAXX can distinguish the two with high precision. By a combination of structural, biochemical and cell-based targeting analyses, we show that Ala87 and Gly90 are the principal determinants of human H3.3 specificity. DAXX uses a shallow hydrophobic pocket to accommodate the small hydrophobic Ala87 of H3.3, whereas a polar binding environment in DAXX prefers Gly90 in H3.3 over the hydrophobic Met90 in H3.1. An H3.3-H4 heterodimer is bound by the histone-binding domain of DAXX, which makes extensive contacts with both H3.3 and H4.
-
-	Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.,Liu CP, Xiong C, Wang M, Yu Z, Yang N, Chen P, Zhang Z, Li G, Xu RM Nat Struct Mol Biol. 2012 Dec;19(12):1287-92. doi: 10.1038/nsmb.2439. Epub 2012, Nov 11. PMID:23142979<ref>PMID:23142979</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4hga" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 08:14, 3 November 2022

OCA — Thu, 03 Nov 2022 08:14:44 GMT

←Older revision		Revision as of 08:14, 3 November 2022
Line 1:		Line 1:

	==Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX==		==Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX==
-	<StructureSection load='4hga' size='340' side='right' caption='[[4hga]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='4hga' size='340' side='right'caption='[[4hga]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hga]] 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=4HGA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HGA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hga]] 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=4HGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAXX, BING2, DAP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [https://pdbe.org/4hga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [https://www.ebi.ac.uk/pdbsum/4hga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hga 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=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [~~http~~://pdbe.org/4hga PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hga PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hga ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DAXX_HUMAN DAXX_HUMAN]] Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.<ref>PMID:12140263</ref> <ref>PMID:15364927</ref> <ref>PMID:17081986</ref> <ref>PMID:16845383</ref>	+	[https://www.uniprot.org/uniprot/DAXX_HUMAN DAXX_HUMAN] Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.<ref>PMID:12140263</ref> <ref>PMID:15364927</ref> <ref>PMID:17081986</ref> <ref>PMID:16845383</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 20:

	==See Also==		==See Also==
-	*[[Death-associated protein\|Death-associated protein]]	+	*[[Death-associated protein 3D structures\|Death-associated protein 3D structures]]
-	*[[Histone\|Histone]]	+	*[[Histone 3D structures\|Histone 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Chen, P]]	+	[[Category: Large Structures]]
-	[[Category: Li~~, G H~~]]	+	[[Category: Chen P]]
-	[[Category: Liu~~, C P~~]]	+	[[Category: Li GH]]
-	[[Category: Wang~~, M Z~~]]	+	[[Category: Liu CP]]
-	[[Category: Xiong~~, C Y~~]]	+	[[Category: Wang MZ]]
-	[[Category: Xu~~, R M~~]]	+	[[Category: Xiong CY]]
-	[[Category: Yang, N]]	+	[[Category: Xu RM]]
-	[[Category: Yu~~, Z L~~]]	+	[[Category: Yang N]]
-	[[Category: Zhang~~, Z G]]~~	+	[[Category: Yu ZL]]
-	~~[[Category: Chaperone-apoptosis complex]]~~	+	[[Category: Zhang ZG]]
-	~~[[Category: Histone chaperone~~]]	+

OCA at 15:45, 4 August 2016

OCA — Thu, 04 Aug 2016 15:45:42 GMT

←Older revision		Revision as of 15:45, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX==		==Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX==
	<StructureSection load='4hga' size='340' side='right' caption='[[4hga]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='4hga' size='340' side='right' caption='[[4hga]], [[Resolution\|resolution]] 2.80Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAXX, BING2, DAP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([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">DAXX, BING2, DAP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([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=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [http://www.ebi.ac.uk/pdbsum/4hga 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=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [http://pdbe.org/4hga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [http://www.ebi.ac.uk/pdbsum/4hga PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hga ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4hga" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 10:41, 25 December 2014

OCA — Thu, 25 Dec 2014 10:41:29 GMT

←Older revision		Revision as of 10:41, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hga]] 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=4HGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HGA FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hga]] 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=4HGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HGA FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAXX, BING2, DAP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([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">DAXX, BING2, DAP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [http://www.ebi.ac.uk/pdbsum/4hga 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=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [http://www.ebi.ac.uk/pdbsum/4hga PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DAXX_HUMAN DAXX_HUMAN]] Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.<ref>PMID:12140263</ref> <ref>PMID:15364927</ref> <ref>PMID:17081986</ref> <ref>PMID:16845383</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Chen, P.]]	+	[[Category: Chen, P]]
-	[[Category: Li, G H.]]	+	[[Category: Li, G H]]
-	[[Category: Liu, C P.]]	+	[[Category: Liu, C P]]
-	[[Category: Wang, M Z.]]	+	[[Category: Wang, M Z]]
-	[[Category: Xiong, C Y.]]	+	[[Category: Xiong, C Y]]
-	[[Category: Xu, R M.]]	+	[[Category: Xu, R M]]
-	[[Category: Yang, N.]]	+	[[Category: Yang, N]]
-	[[Category: Yu, Z L.]]	+	[[Category: Yu, Z L]]
-	[[Category: Zhang, Z G.]]	+	[[Category: Zhang, Z G]]
	[[Category: Chaperone-apoptosis complex]]		[[Category: Chaperone-apoptosis complex]]
	[[Category: Histone chaperone]]		[[Category: Histone chaperone]]

OCA at 07:26, 10 September 2014

OCA — Wed, 10 Sep 2014 07:26:36 GMT

←Older revision		Revision as of 07:26, 10 September 2014
Line 1:		Line 1:
-	[[~~Image:~~4hga.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX==
		+	<StructureSection load='4hga' size='340' side='right' caption='[[4hga]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4hga]] 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=4HGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HGA FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DAXX, BING2, DAP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hga OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hga RCSB], [http://www.ebi.ac.uk/pdbsum/4hga PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mammalian histone H3.3 is a variant of the canonical H3.1 essential for genome reprogramming in fertilized eggs and maintenance of chromatin structure in neuronal cells. An H3.3-specific histone chaperone, DAXX, directs the deposition of H3.3 onto pericentric and telomeric heterochromatin. H3.3 differs from H3.1 by only five amino acids, yet DAXX can distinguish the two with high precision. By a combination of structural, biochemical and cell-based targeting analyses, we show that Ala87 and Gly90 are the principal determinants of human H3.3 specificity. DAXX uses a shallow hydrophobic pocket to accommodate the small hydrophobic Ala87 of H3.3, whereas a polar binding environment in DAXX prefers Gly90 in H3.3 over the hydrophobic Met90 in H3.1. An H3.3-H4 heterodimer is bound by the histone-binding domain of DAXX, which makes extensive contacts with both H3.3 and H4.

-	~~{{STRUCTURE_4hga\| PDB=4hga \| SCENE= }}~~	+	Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.,Liu CP, Xiong C, Wang M, Yu Z, Yang N, Chen P, Zhang Z, Li G, Xu RM Nat Struct Mol Biol. 2012 Dec;19(12):1287-92. doi: 10.1038/nsmb.2439. Epub 2012, Nov 11. PMID:23142979<ref>PMID:23142979</ref>

-	~~===Structure~~ of the ~~variant histone H3~~.~~3-H4 heterodimer in complex with its chaperone DAXX===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	==~~About this Structure~~==	+	*[[Death-associated protein\|Death-associated protein]]
-	[[~~4hga~~]] ~~is a 3 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=4HGA OCA].~~	+	*[[Histone\|Histone]]
-	[[Category: ~~Homo sapiens~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Chen, P.]]		[[Category: Chen, P.]]
	[[Category: Li, G H.]]		[[Category: Li, G H.]]

OCA at 14:05, 8 November 2012

OCA — Thu, 08 Nov 2012 14:05:52 GMT

←Older revision		Revision as of 14:05, 8 November 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4hga.jpg\|left\|200px]]

-	~~The entry~~ 4hga ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4hga\| PDB=4hga \| SCENE= }}

-	~~Authors: Liu, C.P., Xiong, C.Y., Wang, M.Z., Yu, Z.L., Yang, N., Chen, P., Zhang, Z.G., Li, G.H., Xu, R.M~~.	+	===Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX===

-	~~Description:~~ Structure ~~of the variant histone H3.~~3-~~H4 heterodimer in~~ complex ~~with its~~ chaperone ~~DAXX~~	+
		+	==About this Structure==
		+	[[4hga]] is a 3 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=4HGA OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Chen, P.]]
		+	[[Category: Li, G H.]]
		+	[[Category: Liu, C P.]]
		+	[[Category: Wang, M Z.]]
		+	[[Category: Xiong, C Y.]]
		+	[[Category: Xu, R M.]]
		+	[[Category: Yang, N.]]
		+	[[Category: Yu, Z L.]]
		+	[[Category: Zhang, Z G.]]
		+	[[Category: Chaperone-apoptosis complex]]
		+	[[Category: Histone chaperone]]

OCA at 08:38, 31 October 2012

OCA — Wed, 31 Oct 2012 08:38:55 GMT

←Older revision		Revision as of 08:38, 31 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Liu, C.P., Xiong, C.Y., Wang, M.Z., Yu, Z.L., Yang, N., Chen, P., Zhang, Z.G., Li, G.H., Xu, R.M.		Authors: Liu, C.P., Xiong, C.Y., Wang, M.Z., Yu, Z.L., Yang, N., Chen, P., Zhang, Z.G., Li, G.H., Xu, R.M.

	Description: Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX		Description: Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX

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

OCA — Wed, 17 Oct 2012 06:36:41 GMT

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

←Older revision

Revision as of 06:36, 17 October 2012

OCA: New page: '''Unreleased structure''' The entry 4hga is ON HOLD Authors: Liu, C.P., Xiong, C.Y., Wang, M.Z., Yu, Z.L., Yang, N., Chen, P., Zhang, Z.G., Li, G.H., Xu, R.M. Description: Structure o...

OCA — Wed, 17 Oct 2012 06:36:40 GMT

New page: '''Unreleased structure''' The entry 4hga is ON HOLD Authors: Liu, C.P., Xiong, C.Y., Wang, M.Z., Yu, Z.L., Yang, N., Chen, P., Zhang, Z.G., Li, G.H., Xu, R.M. Description: Structure o...

New page

'''Unreleased structure'''

The entry 4hga is ON HOLD

Authors: Liu, C.P., Xiong, C.Y., Wang, M.Z., Yu, Z.L., Yang, N., Chen, P., Zhang, Z.G., Li, G.H., Xu, R.M.

Description: Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX