5fpg - Revision history

OCA at 13:17, 26 July 2023

2023-07-26T13:17:24Z

← Older revision		Revision as of 13:17, 26 July 2023
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	<StructureSection load='5fpg' size='340' side='right'caption='[[5fpg]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='5fpg' size='340' side='right'caption='[[5fpg]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5fpg]] 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=5FPG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FPG FirstGlance]. <br>		<table><tr><td colspan='2'>[[5fpg]] 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=5FPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FPG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=Q28:4-[3-(8-METHYL-4-OXO-3,4-DIHYDROQUINAZOLIN-2-+YL)PROPANAMIDO]-N-(QUINOLIN-8-YL)BENZAMIDE'>Q28</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]] 2.75Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5fpf\|5fpf]]~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=Q28:4-[3-(8-METHYL-4-OXO-3,4-DIHYDROQUINAZOLIN-2-+YL)PROPANAMIDO]-N-(QUINOLIN-8-YL)BENZAMIDE'>Q28</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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5fpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fpg OCA], [~~http~~://pdbe.org/5fpg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5fpg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5fpg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5fpg 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=5fpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fpg OCA], [https://pdbe.org/5fpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fpg RCSB], [https://www.ebi.ac.uk/pdbsum/5fpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fpg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/TNKS2_HUMAN TNKS2_HUMAN]] Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.<ref>PMID:11802774</ref> <ref>PMID:11739745</ref> <ref>PMID:19759537</ref> <ref>PMID:21478859</ref>		[https://www.uniprot.org/uniprot/TNKS2_HUMAN TNKS2_HUMAN] Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.<ref>PMID:11802774</ref> <ref>PMID:11739745</ref> <ref>PMID:19759537</ref> <ref>PMID:21478859</ref>

	==See Also==		==See Also==
	*[[Poly (ADP-ribose) polymerase\|Poly (ADP-ribose) polymerase]]		*[[Poly(ADP-ribose) polymerase 3D structures\|Poly(ADP-ribose) polymerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Haikarainen, T]]		[[Category: Haikarainen T]]
	[[Category: Lehtio, L]]		[[Category: Lehtio L]]
	~~[[Category: Adp- ribosylation]]~~
	~~[[Category: Diphtheria toxin like fold]]~~
	~~[[Category: Protein-ligand complex]]~~
	~~[[Category: Transferase]]~~
	~~[[Category: Transferase-transferase inhibitor complex~~]]

OCA at 07:34, 23 October 2019

2019-10-23T07:34:52Z

← Older revision		Revision as of 07:34, 23 October 2019
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	==Crystal structure of human tankyrase 2 in complex with TA-92==		==Crystal structure of human tankyrase 2 in complex with TA-92==
	<StructureSection load='5fpg' size='340' side='right' caption='[[5fpg]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='5fpg' size='340' side='right'caption='[[5fpg]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5fpg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FPG FirstGlance]. <br>		<table><tr><td colspan='2'>[[5fpg]] 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=5FPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FPG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=Q28:4-[3-(8-METHYL-4-OXO-3,4-DIHYDROQUINAZOLIN-2-+YL)PROPANAMIDO]-N-(QUINOLIN-8-YL)BENZAMIDE'>Q28</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=Q28:4-[3-(8-METHYL-4-OXO-3,4-DIHYDROQUINAZOLIN-2-+YL)PROPANAMIDO]-N-(QUINOLIN-8-YL)BENZAMIDE'>Q28</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">[[5fpf\|5fpf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5fpf\|5fpf]]</td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Haikarainen, T]]		[[Category: Haikarainen, T]]
	[[Category: Lehtio, L]]		[[Category: Lehtio, L]]

OCA at 06:53, 6 October 2017

2017-10-06T06:53:09Z

← Older revision		Revision as of 06:53, 6 October 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/TNKS2_HUMAN TNKS2_HUMAN]] Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.<ref>PMID:11802774</ref> <ref>PMID:11739745</ref> <ref>PMID:19759537</ref> <ref>PMID:21478859</ref>		[[http://www.uniprot.org/uniprot/TNKS2_HUMAN TNKS2_HUMAN]] Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.<ref>PMID:11802774</ref> <ref>PMID:11739745</ref> <ref>PMID:19759537</ref> <ref>PMID:21478859</ref>

			==See Also==
			*[[Poly (ADP-ribose) polymerase\|Poly (ADP-ribose) polymerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:15, 15 December 2016

2016-12-15T19:15:01Z

← Older revision		Revision as of 19:15, 15 December 2016
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	~~'''Unreleased structure'''~~

	~~The entry~~ 5fpg is ~~ON HOLD until Paper Publication~~		==Crystal structure of human tankyrase 2 in complex with TA-92==
			<StructureSection load='5fpg' size='340' side='right' caption='[[5fpg]], [[Resolution\|resolution]] 2.75Å' scene=''>
	~~Authors~~: ~~Haikarainen~~, T., ~~Lehtio~~, L.		== Structural highlights ==
			<table><tr><td colspan='2'>[[5fpg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FPG FirstGlance]. <br>
	~~Description~~: ~~Crystal structure~~ of ~~human tankyrase~~ 2 in complex ~~with TA~~-92		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=Q28:4-[3-(8-METHYL-4-OXO-3,4-DIHYDROQUINAZOLIN-2-+YL)PROPANAMIDO]-N-(QUINOLIN-8-YL)BENZAMIDE'>Q28</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	[[Category: ~~Unreleased Structures~~]]		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5fpf\|5fpf]]</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=5fpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fpg OCA], [http://pdbe.org/5fpg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fpg RCSB], [http://www.ebi.ac.uk/pdbsum/5fpg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fpg ProSAT]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/TNKS2_HUMAN TNKS2_HUMAN]] Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.<ref>PMID:11802774</ref> <ref>PMID:11739745</ref> <ref>PMID:19759537</ref> <ref>PMID:21478859</ref>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Haikarainen, T]]
	[[Category: Lehtio, L]]		[[Category: Lehtio, L]]
	[[Category: ~~Haikarainen, T~~]]		[[Category: Adp- ribosylation]]
			[[Category: Diphtheria toxin like fold]]
			[[Category: Protein-ligand complex]]
			[[Category: Transferase]]
			[[Category: Transferase-transferase inhibitor complex]]

OCA at 12:59, 16 December 2015

2015-12-16T12:59:50Z

← Older revision		Revision as of 12:59, 16 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 5fpg is ON HOLD		The entry 5fpg is ON HOLD until Paper Publication

	Authors: Haikarainen, T., Lehtio, L.		Authors: Haikarainen, T., Lehtio, L.

OCA: Protected "5fpg" [edit=sysop:move=sysop]

2015-12-09T12:52:09Z

Protected "5fpg" [edit=sysop:move=sysop]

← Older revision	Revision as of 12:52, 9 December 2015
(No difference)

OCA: New page: '''Unreleased structure''' The entry 5fpg is ON HOLD Authors: Haikarainen, T., Lehtio, L. Description: Crystal structure of human tankyrase 2 in complex with TA-92 [[Category: Unreleas...

2015-12-09T12:52:08Z

New page: '''Unreleased structure''' The entry 5fpg is ON HOLD Authors: Haikarainen, T., Lehtio, L. Description: Crystal structure of human tankyrase 2 in complex with TA-92 [[Category: Unreleas...

New page

'''Unreleased structure'''

The entry 5fpg is ON HOLD

Authors: Haikarainen, T., Lehtio, L.

Description: Crystal structure of human tankyrase 2 in complex with TA-92
[[Category: Unreleased Structures]]
[[Category: Lehtio, L]]
[[Category: Haikarainen, T]]