2xoy - Revision history

OCA at 10:36, 20 December 2023

2023-12-20T10:36:07Z

←Older revision		Revision as of 10:36, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='2xoy' size='340' side='right'caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='2xoy' size='340' side='right'caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xoy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XOY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xoy]] is a 2 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=2XOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XOY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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]] 2.6Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [https://pdbe.org/2xoy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [https://www.ebi.ac.uk/pdbsum/2xoy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xoy 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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [https://pdbe.org/2xoy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [https://www.ebi.ac.uk/pdbsum/2xoy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xoy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CHFR_HUMAN CHFR_HUMAN]] E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.<ref>PMID:10935642</ref> <ref>PMID:11807090</ref> <ref>PMID:11912157</ref> <ref>PMID:14562038</ref> <ref>PMID:14694445</ref> <ref>PMID:18172500</ref> <ref>PMID:19182791</ref>	+	[https://www.uniprot.org/uniprot/CHFR_HUMAN CHFR_HUMAN] E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.<ref>PMID:10935642</ref> <ref>PMID:11807090</ref> <ref>PMID:11912157</ref> <ref>PMID:14562038</ref> <ref>PMID:14694445</ref> <ref>PMID:18172500</ref> <ref>PMID:19182791</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bayliss, R]]	+	[[Category: Bayliss R]]
-	[[Category: Oberoi, J]]	+	[[Category: Oberoi J]]
-	~~[[Category: Antephase checkpoint]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Mitosis]]~~	+
-	~~[[Category: Pbz]]~~	+
-	~~[[Category: Zinc-binding~~]]	+

OCA at 12:14, 27 April 2022

2022-04-27T12:14:47Z

←Older revision		Revision as of 12:14, 27 April 2022
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	<StructureSection load='2xoy' size='340' side='right'caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='2xoy' size='340' side='right'caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xoy]] is a 2 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=2XOY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2XOY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xoy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XOY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [~~http~~://pdbe.org/2xoy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2xoy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2xoy 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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [https://pdbe.org/2xoy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [https://www.ebi.ac.uk/pdbsum/2xoy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xoy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CHFR_HUMAN CHFR_HUMAN]] E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.<ref>PMID:10935642</ref> <ref>PMID:11807090</ref> <ref>PMID:11912157</ref> <ref>PMID:14562038</ref> <ref>PMID:14694445</ref> <ref>PMID:18172500</ref> <ref>PMID:19182791</ref>	+	[[https://www.uniprot.org/uniprot/CHFR_HUMAN CHFR_HUMAN]] E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.<ref>PMID:10935642</ref> <ref>PMID:11807090</ref> <ref>PMID:11912157</ref> <ref>PMID:14562038</ref> <ref>PMID:14694445</ref> <ref>PMID:18172500</ref> <ref>PMID:19182791</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:15, 22 July 2020

2020-07-22T12:15:13Z

←Older revision		Revision as of 12:15, 22 July 2020
Line 1:		Line 1:

	==C-terminal cysteine-rich domain of human CHFR bound to P(1),P(2)- Diadenosine-5'-pyrophosphate==		==C-terminal cysteine-rich domain of human CHFR bound to P(1),P(2)- Diadenosine-5'-pyrophosphate==
-	<StructureSection load='2xoy' size='340' side='right' caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='2xoy' size='340' side='right'caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xoy]] is a 2 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=2XOY OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2XOY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xoy]] is a 2 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=2XOY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XOY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [http://pdbe.org/2xoy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [http://www.ebi.ac.uk/pdbsum/2xoy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xoy ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [http://pdbe.org/2xoy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [http://www.ebi.ac.uk/pdbsum/2xoy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xoy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]	+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bayliss, R]]		[[Category: Bayliss, R]]
	[[Category: Oberoi, J]]		[[Category: Oberoi, J]]

OCA at 08:53, 10 October 2018

2018-10-10T08:53:22Z

←Older revision		Revision as of 08:53, 10 October 2018
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-	==C-~~TERMINAL CYSTEINE~~-~~RICH DOMAIN OF HUMAN~~ CHFR ~~BOUND TO~~ P(1), P(2)-~~DIADENOSINE~~-5'-~~PYROPHOSPHATE~~==	+	==C-terminal cysteine-rich domain of human CHFR bound to P(1),P(2)- Diadenosine-5'-pyrophosphate==
	<StructureSection load='2xoy' size='340' side='right' caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='2xoy' size='340' side='right' caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xo/2xoy_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xo/2xoy_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>

OCA at 13:26, 4 August 2016

2016-08-04T13:26:59Z

←Older revision		Revision as of 13:26, 4 August 2016
Line 1:		Line 1:
		+
	==C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE==		==C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE==
	<StructureSection load='2xoy' size='340' side='right' caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='2xoy' size='340' side='right' caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2xoy]] is a 2 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=2XOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XOY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2xoy]] is a 2 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=2XOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XOY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [http://www.ebi.ac.uk/pdbsum/2xoy 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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [http://pdbe.org/2xoy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [http://www.ebi.ac.uk/pdbsum/2xoy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xoy 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=2xoy 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 2xoy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bayliss, R]]		[[Category: Bayliss, R]]
	[[Category: Oberoi, J]]		[[Category: Oberoi, J]]

OCA at 09:42, 25 December 2014

2014-12-25T09:42:55Z

←Older revision		Revision as of 09:42, 25 December 2014
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	<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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [http://www.ebi.ac.uk/pdbsum/2xoy 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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [http://www.ebi.ac.uk/pdbsum/2xoy PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CHFR_HUMAN CHFR_HUMAN]] E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.<ref>PMID:10935642</ref> <ref>PMID:11807090</ref> <ref>PMID:11912157</ref> <ref>PMID:14562038</ref> <ref>PMID:14694445</ref> <ref>PMID:18172500</ref> <ref>PMID:19182791</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:32, 18 December 2014

2014-12-18T11:32:49Z

←Older revision		Revision as of 11:32, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2xoy\| PDB=2xoy \| SCENE= }}~~	+	==C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE==
-	===C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE===	+	<StructureSection load='2xoy' size='340' side='right' caption='[[2xoy]], [[Resolution\|resolution]] 2.60Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20880844}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2xoy]] is a 2 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=2XOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XOY FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2xoc\|2xoc]], [[1lgp\|1lgp]], [[2xoz\|2xoz]], [[2xp0\|2xp0]], [[1lgq\|1lgq]]</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=2xoy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xoy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xoy RCSB], [http://www.ebi.ac.uk/pdbsum/2xoy 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/xo/2xoy_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 ==
		+	Cellular stress in early mitosis activates the antephase checkpoint, resulting in the decondensation of chromosomes and delayed mitotic progression. Checkpoint with forkhead-associated and RING domains (CHFR) is central to this checkpoint, and its activity is ablated in many tumors and cancer cell lines through promoter hypermethylation or mutation. The interaction between the PAR-binding zinc finger (PBZ) of CHFR and poly(ADP-ribose) (PAR) is crucial for a functional antephase checkpoint. We determined the crystal structure of the cysteine-rich region of human CHFR (amino acids 425-664) to 1.9 A resolution, which revealed a multizinc binding domain of elaborate topology within which the PBZ is embedded. The PBZ of CHFR closely resembles the analogous motifs from aprataxin-like factor and CG1218-PA, which lie within unstructured regions of their respective proteins. Based on co-crystal structures of CHFR bound to several different PAR-like ligands (adenosine 5'-diphosphoribose, adenosine monophosphate, and P(1)P(2)-diadenosine 5'-pyrophosphate), we made a model of the CHFR-PAR interaction, which we validated using site-specific mutagenesis and surface plasmon resonance. The PBZ motif of CHFR recognizes two adenine-containing subunits of PAR and the phosphate backbone that connects them. More generally, PBZ motifs may recognize different numbers of PAR subunits as required to carry out their functions.

-	~~==Function==~~	+	Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR).,Oberoi J, Richards MW, Crumpler S, Brown N, Blagg J, Bayliss R J Biol Chem. 2010 Dec 10;285(50):39348-58. Epub 2010 Sep 29. PMID:20880844<ref>PMID:20880844</ref>
-	~~[[http://www.uniprot.org/uniprot/CHFR_HUMAN CHFR_HUMAN]] E3 ubiquitin~~-~~protein ligase that functions in the antephase checkpoint~~ by ~~actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when~~ the ~~centrosome move apart from each other along the periphery~~ of ~~the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys~~-~~48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination~~ and ~~subsequent degradation of AURKA and PLK1~~. ~~Probably acts as a tumor suppressor~~, ~~possibly by mediating the polyubiquitination of HDAC1~~, ~~leading to its degradation~~. ~~May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2~~ (~~UBE2N-UBE2V2~~) ~~heterodimer. Substrates that are polyubiquitinated at 'Lys~~-~~63' are usually not targeted for degradation, but are rather involved in signaling cellular stress~~.~~<ref>~~PMID:~~10935642</ref> <ref>PMID:11807090</ref> <ref>PMID:11912157</ref> <ref>PMID:14562038</ref> <ref>PMID:14694445</ref> <ref>PMID:18172500</ref>~~ <ref>PMID:~~19182791~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[2xoy]] is~~ a ~~2 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=2XOY OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]		*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020880844</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bayliss, R.]]	+	[[Category: Bayliss, R]]
-	[[Category: Oberoi, J.]]	+	[[Category: Oberoi, J]]
	[[Category: Antephase checkpoint]]		[[Category: Antephase checkpoint]]
	[[Category: Ligase]]		[[Category: Ligase]]

OCA at 20:50, 17 April 2013

2013-04-17T20:50:02Z

←Older revision		Revision as of 20:50, 17 April 2013
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-	[[Image:2xoy.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_2xoy", 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_2xoy\| PDB=2xoy \| SCENE= }}		{{STRUCTURE_2xoy\| PDB=2xoy \| SCENE= }}
-
	===C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE===		===C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE===
		+	{{ABSTRACT_PUBMED_20880844}}

-		+	==Function==
-	~~<!--~~	+	[[http://www.uniprot.org/uniprot/CHFR_HUMAN CHFR_HUMAN]] E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.<ref>PMID:10935642</ref> <ref>PMID:11807090</ref> <ref>PMID:11912157</ref> <ref>PMID:14562038</ref> <ref>PMID:14694445</ref> <ref>PMID:18172500</ref> <ref>PMID:19182791</ref>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_20880844}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 20880844 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20880844}}~~	+

	==About this Structure==		==About this Structure==
	[[2xoy]] is a 2 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=2XOY OCA].		[[2xoy]] is a 2 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=2XOY OCA].
		+
		+	==See Also==
		+	*[[Ubiquitin protein ligase\|Ubiquitin protein ligase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020880844</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020880844</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bayliss, R.]]		[[Category: Bayliss, R.]]

OCA: Protected "2xoy" [edit=sysop:move=sysop]

2011-06-15T05:24:41Z

Protected "2xoy" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:24, 15 June 2011

OCA at 05:24, 15 June 2011

2011-06-15T05:24:40Z

←Older revision		Revision as of 05:24, 15 June 2011
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-	~~{{Seed}}~~	+	[[Image:2xoy.png\|left\|200px]]
-	[[Image:2xoy.~~jpg~~\|left\|200px]]	+

	<!--		<!--
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	===C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE===		===C-TERMINAL CYSTEINE-RICH DOMAIN OF HUMAN CHFR BOUND TO P(1), P(2)-DIADENOSINE-5'-PYROPHOSPHATE===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20880844}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20880844 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20880844}}

	==About this Structure==		==About this Structure==
-	~~2XOY~~ is a 2 ~~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=2XOY OCA].	+	[[2xoy]] is a 2 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=2XOY OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:020880844</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bayliss, R.]]		[[Category: Bayliss, R.]]
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	[[Category: Pbz]]		[[Category: Pbz]]
	[[Category: Zinc-binding]]		[[Category: Zinc-binding]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 29 08:11:05 2010''