6imq - Revision history

OCA at 10:33, 27 March 2024

OCA — Wed, 27 Mar 2024 10:33:59 GMT

←Older revision		Revision as of 10:33, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='6imq' size='340' side='right'caption='[[6imq]], [[Resolution\|resolution]] 2.06Å' scene=''>		<StructureSection load='6imq' size='340' side='right'caption='[[6imq]], [[Resolution\|resolution]] 2.06Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6imq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IMQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6IMQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6imq]] is a 4 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=6IMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IMQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.06Å</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=6imq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6imq OCA], [~~http~~://pdbe.org/6imq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6imq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6imq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6imq ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6imq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6imq OCA], [https://pdbe.org/6imq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6imq RCSB], [https://www.ebi.ac.uk/pdbsum/6imq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6imq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN]] Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon.<ref>PMID:1652369</ref> <ref>PMID:1720570</ref>	+	[https://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN] Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon.<ref>PMID:1652369</ref> <ref>PMID:1720570</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN]] Key component of PML nuclear bodies that regulate a large number of cellular processes by facilitating post-translational modification of target proteins, promoting protein-protein contacts, or by sequestering proteins. Functions as tumor suppressor. Required for normal, caspase-dependent apoptosis in response to DNA damage, FAS, TNF, or interferons. Plays a role in transcription regulation, DNA damage response, DNA repair and chromatin organization. Plays a role in processes regulated by retinoic acid, regulation of cell division, terminal differentiation of myeloid precursor cells and differentiation of neural progenitor cells. Required for normal immunity to microbial infections. Plays a role in antiviral response. In the cytoplasm, plays a role in TGFB1-dependent processes. Regulates p53/TP53 levels by inhibiting its ubiquitination and proteasomal degradation. Regulates activation of p53/TP53 via phosphorylation at 'Ser-20'. Sequesters MDM2 in the nucleolus after DNA damage, and thereby inhibits ubiquitination and degradation of p53/TP53. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates RB1 phosphorylation and activity. Required for normal development of the brain cortex during embryogenesis. Can sequester herpes virus and varicella virus proteins inside PML bodies, and thereby inhibit the formation of infectious viral particles. Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum (By similarity). Regulates transcription activity of ELF4. Inhibits specifically the activity of the tetrameric form of PKM. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Regulates PTEN compartmentalization through the inhibition of USP7-mediated deubiquitination.<ref>PMID:9756909</ref> <ref>PMID:10610177</ref> <ref>PMID:10684855</ref> <ref>PMID:11025664</ref> <ref>PMID:11432836</ref> <ref>PMID:12402044</ref> <ref>PMID:12439746</ref> <ref>PMID:12810724</ref> <ref>PMID:14976184</ref> <ref>PMID:15195100</ref> <ref>PMID:15356634</ref> <ref>PMID:17030982</ref> <ref>PMID:18298799</ref> <ref>PMID:18716620</ref> <ref>PMID:17173041</ref> <ref>PMID:19567472</ref> <ref>PMID:21172801</ref> <ref>PMID:21304940</ref>	+	[https://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN] Key component of PML nuclear bodies that regulate a large number of cellular processes by facilitating post-translational modification of target proteins, promoting protein-protein contacts, or by sequestering proteins. Functions as tumor suppressor. Required for normal, caspase-dependent apoptosis in response to DNA damage, FAS, TNF, or interferons. Plays a role in transcription regulation, DNA damage response, DNA repair and chromatin organization. Plays a role in processes regulated by retinoic acid, regulation of cell division, terminal differentiation of myeloid precursor cells and differentiation of neural progenitor cells. Required for normal immunity to microbial infections. Plays a role in antiviral response. In the cytoplasm, plays a role in TGFB1-dependent processes. Regulates p53/TP53 levels by inhibiting its ubiquitination and proteasomal degradation. Regulates activation of p53/TP53 via phosphorylation at 'Ser-20'. Sequesters MDM2 in the nucleolus after DNA damage, and thereby inhibits ubiquitination and degradation of p53/TP53. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates RB1 phosphorylation and activity. Required for normal development of the brain cortex during embryogenesis. Can sequester herpes virus and varicella virus proteins inside PML bodies, and thereby inhibit the formation of infectious viral particles. Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum (By similarity). Regulates transcription activity of ELF4. Inhibits specifically the activity of the tetrameric form of PKM. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Regulates PTEN compartmentalization through the inhibition of USP7-mediated deubiquitination.<ref>PMID:9756909</ref> <ref>PMID:10610177</ref> <ref>PMID:10684855</ref> <ref>PMID:11025664</ref> <ref>PMID:11432836</ref> <ref>PMID:12402044</ref> <ref>PMID:12439746</ref> <ref>PMID:12810724</ref> <ref>PMID:14976184</ref> <ref>PMID:15195100</ref> <ref>PMID:15356634</ref> <ref>PMID:17030982</ref> <ref>PMID:18298799</ref> <ref>PMID:18716620</ref> <ref>PMID:17173041</ref> <ref>PMID:19567472</ref> <ref>PMID:21172801</ref> <ref>PMID:21304940</ref>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cai, X]]	+	[[Category: Cai X]]
-	[[Category: Chen~~, S J~~]]	+	[[Category: Chen SJ]]
-	[[Category: Chen, Z]]	+	[[Category: Chen Z]]
-	[[Category: Cheng, N]]	+	[[Category: Cheng N]]
-	[[Category: Li, Y]]	+	[[Category: Li Y]]
-	[[Category: Ma, X]]	+	[[Category: Ma X]]
-	[[Category: Meng, G]]	+	[[Category: Meng G]]
-	[[Category: Wang, P]]	+	[[Category: Wang P]]
-	[[Category: Wu, H]]	+	[[Category: Wu H]]
-	[[Category: Wu, W]]	+	[[Category: Wu W]]
-	[[Category: Zeng, L]]	+	[[Category: Zeng L]]
-	[[Category: Zhang, H]]	+	[[Category: Zhang H]]
-	~~[[Category: Apl]]~~	+
-	~~[[Category: B1-box]]~~	+
-	~~[[Category: Leukemia]]~~	+
-	~~[[Category: Nuclear body]]~~	+
-	~~[[Category: Oncoprotein]]~~	+
-	~~[[Category: Pml]]~~	+
-	~~[[Category: Pml-rara]]~~	+
-	~~[[Category: Trim19~~]]	+

OCA at 06:17, 31 July 2019

OCA — Wed, 31 Jul 2019 06:17:39 GMT

←Older revision		Revision as of 06:17, 31 July 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6imq is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of PML B1-box multimers==
-		+	<StructureSection load='6imq' size='340' side='right'caption='[[6imq]], [[Resolution\|resolution]] 2.06Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6imq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IMQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IMQ FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6imq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6imq OCA], [http://pdbe.org/6imq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6imq RCSB], [http://www.ebi.ac.uk/pdbsum/6imq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6imq ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN]] Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon.<ref>PMID:1652369</ref> <ref>PMID:1720570</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN]] Key component of PML nuclear bodies that regulate a large number of cellular processes by facilitating post-translational modification of target proteins, promoting protein-protein contacts, or by sequestering proteins. Functions as tumor suppressor. Required for normal, caspase-dependent apoptosis in response to DNA damage, FAS, TNF, or interferons. Plays a role in transcription regulation, DNA damage response, DNA repair and chromatin organization. Plays a role in processes regulated by retinoic acid, regulation of cell division, terminal differentiation of myeloid precursor cells and differentiation of neural progenitor cells. Required for normal immunity to microbial infections. Plays a role in antiviral response. In the cytoplasm, plays a role in TGFB1-dependent processes. Regulates p53/TP53 levels by inhibiting its ubiquitination and proteasomal degradation. Regulates activation of p53/TP53 via phosphorylation at 'Ser-20'. Sequesters MDM2 in the nucleolus after DNA damage, and thereby inhibits ubiquitination and degradation of p53/TP53. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates RB1 phosphorylation and activity. Required for normal development of the brain cortex during embryogenesis. Can sequester herpes virus and varicella virus proteins inside PML bodies, and thereby inhibit the formation of infectious viral particles. Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum (By similarity). Regulates transcription activity of ELF4. Inhibits specifically the activity of the tetrameric form of PKM. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Regulates PTEN compartmentalization through the inhibition of USP7-mediated deubiquitination.<ref>PMID:9756909</ref> <ref>PMID:10610177</ref> <ref>PMID:10684855</ref> <ref>PMID:11025664</ref> <ref>PMID:11432836</ref> <ref>PMID:12402044</ref> <ref>PMID:12439746</ref> <ref>PMID:12810724</ref> <ref>PMID:14976184</ref> <ref>PMID:15195100</ref> <ref>PMID:15356634</ref> <ref>PMID:17030982</ref> <ref>PMID:18298799</ref> <ref>PMID:18716620</ref> <ref>PMID:17173041</ref> <ref>PMID:19567472</ref> <ref>PMID:21172801</ref> <ref>PMID:21304940</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Cai, X]]
		+	[[Category: Chen, S J]]
		+	[[Category: Chen, Z]]
		+	[[Category: Cheng, N]]
		+	[[Category: Li, Y]]
		+	[[Category: Ma, X]]
		+	[[Category: Meng, G]]
		+	[[Category: Wang, P]]
		+	[[Category: Wu, H]]
		+	[[Category: Wu, W]]
		+	[[Category: Zeng, L]]
		+	[[Category: Zhang, H]]
		+	[[Category: Apl]]
		+	[[Category: B1-box]]
		+	[[Category: Leukemia]]
		+	[[Category: Nuclear body]]
		+	[[Category: Oncoprotein]]
		+	[[Category: Pml]]
		+	[[Category: Pml-rara]]
		+	[[Category: Trim19]]

OCA at 06:28, 14 November 2018

OCA — Wed, 14 Nov 2018 06:28:20 GMT

←Older revision		Revision as of 06:28, 14 November 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6imq is ON HOLD	+	The entry 6imq is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6imq" [edit=sysop:move=sysop]

OCA — Wed, 31 Oct 2018 05:22:10 GMT

Protected "6imq" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:22, 31 October 2018

OCA: New page: '''Unreleased structure''' The entry 6imq is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 31 Oct 2018 05:22:09 GMT

New page: '''Unreleased structure''' The entry 6imq is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6imq is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]