1dk8 - Revision history

OCA at 06:55, 7 February 2024

OCA — Wed, 07 Feb 2024 06:55:01 GMT

←Older revision		Revision as of 06:55, 7 February 2024
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	<StructureSection load='1dk8' size='340' side='right'caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>		<StructureSection load='1dk8' size='340' side='right'caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.57Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [https://pdbe.org/1dk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [https://www.ebi.ac.uk/pdbsum/1dk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk8 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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [https://pdbe.org/1dk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [https://www.ebi.ac.uk/pdbsum/1dk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[https://omim.org/entry/114550 114550]].<ref>PMID:10700176</ref> <ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[https://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>	+	[https://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[https://omim.org/entry/114550 114550].<ref>PMID:10700176</ref> <ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[https://omim.org/entry/607864 607864]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12192039</ref> <ref>PMID:16601693</ref> <ref>PMID:17210684</ref>	+	[https://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12192039</ref> <ref>PMID:16601693</ref> <ref>PMID:17210684</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1dk8 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=1dk8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Axin and the adenomatous polyposis coli (APC) tumor suppressor protein are components of the Wnt/Wingless growth factor signaling pathway. In the absence of Wnt signal, Axin and APC regulate cytoplasmic levels of the proto-oncogene beta-catenin through the formation of a large complex containing these three proteins, glycogen synthase kinase 3beta (GSK3beta) and several other proteins. Both Axin and APC are known to be critical for beta-catenin regulation, and truncations in APC that eliminate the Axin-binding site result in human cancers. A protease-resistant domain of Axin that contains the APC-binding site is a member of the regulators of G-protein signaling (RGS) superfamily. The crystal structures of this domain alone and in complex with an Axin-binding sequence from APC reveal that the Axin-APC interaction occurs at a conserved groove on a face of the protein that is distinct from the G-protein interface of classical RGS proteins. The molecular interactions observed in the Axin-APC complex provide a rationale for the evolutionary conservation seen in both proteins.
-
-	Structural basis of the Axin-adenomatous polyposis coli interaction.,Spink KE, Polakis P, Weis WI EMBO J. 2000 May 15;19(10):2270-9. PMID:10811618<ref>PMID:10811618</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1dk8" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Polakis, P]]	+	[[Category: Polakis P]]
-	[[Category: Spink~~, K E~~]]	+	[[Category: Spink KE]]
-	[[Category: Weis~~, W I]]~~	+	[[Category: Weis WI]]
-	~~[[Category: Alpha-helix]]~~	+
-	~~[[Category: Pi-helix]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 09:27, 21 July 2021

OCA — Wed, 21 Jul 2021 09:27:59 GMT

OCA at 14:25, 16 October 2019

OCA — Wed, 16 Oct 2019 14:25:44 GMT

←Older revision		Revision as of 14:25, 16 October 2019
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN==		==CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN==
-	<StructureSection load='1dk8' size='340' side='right' caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>	+	<StructureSection load='1dk8' size='340' side='right'caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Axin\|Axin]]	+	*[[Axin 3D structures\|Axin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Polakis, P]]		[[Category: Polakis, P]]
	[[Category: Spink, K E]]		[[Category: Spink, K E]]

OCA at 08:33, 6 December 2017

OCA — Wed, 06 Dec 2017 08:33:49 GMT

←Older revision		Revision as of 08:33, 6 December 2017
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		+
	==CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN==		==CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN==
	<StructureSection load='1dk8' size='340' side='right' caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>		<StructureSection load='1dk8' size='340' side='right' caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [http://pdbe.org/1dk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk8 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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [http://pdbe.org/1dk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/1dk8_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/1dk8_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 00:33, 10 February 2016

OCA — Wed, 10 Feb 2016 00:33:24 GMT

←Older revision		Revision as of 00:33, 10 February 2016
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	<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=1dk8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 03:36, 11 September 2015

OCA — Fri, 11 Sep 2015 03:36:00 GMT

←Older revision		Revision as of 03:36, 11 September 2015
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	<StructureSection load='1dk8' size='340' side='right' caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>		<StructureSection load='1dk8' size='340' side='right' caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk8 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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [http://pdbe.org/1dk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk8 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 1dk8" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Polakis, P]]		[[Category: Polakis, P]]
	[[Category: Spink, K E]]		[[Category: Spink, K E]]

OCA at 23:58, 22 December 2014

OCA — Mon, 22 Dec 2014 23:58:47 GMT

←Older revision		Revision as of 23:58, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk8 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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk8 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[http://omim.org/entry/114550 114550]].<ref>PMID:10700176</ref> <ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[http://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>		[[http://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[http://omim.org/entry/114550 114550]].<ref>PMID:10700176</ref> <ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[http://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>
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	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Polakis, P.]]	+	[[Category: Polakis, P]]
-	[[Category: Spink, K E.]]	+	[[Category: Spink, K E]]
-	[[Category: Weis, W I.]]	+	[[Category: Weis, W I]]
	[[Category: Alpha-helix]]		[[Category: Alpha-helix]]
	[[Category: Pi-helix]]		[[Category: Pi-helix]]
	[[Category: Signaling protein]]		[[Category: Signaling protein]]

OCA at 17:09, 29 September 2014

OCA — Mon, 29 Sep 2014 17:09:57 GMT

←Older revision		Revision as of 17:09, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1dk8\| PDB=1dk8 \| SCENE= }}~~	+	==CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN==
-	===CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN===	+	<StructureSection load='1dk8' size='340' side='right' caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>
-	~~{{ABSTRACT_PUBMED_10811618}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dk8 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[http://omim.org/entry/114550 114550]].<ref>PMID:10700176</ref> <ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[http://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12192039</ref> <ref>PMID:16601693</ref> <ref>PMID:17210684</ref>
		+	== 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/dk/1dk8_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 ==
		+	Axin and the adenomatous polyposis coli (APC) tumor suppressor protein are components of the Wnt/Wingless growth factor signaling pathway. In the absence of Wnt signal, Axin and APC regulate cytoplasmic levels of the proto-oncogene beta-catenin through the formation of a large complex containing these three proteins, glycogen synthase kinase 3beta (GSK3beta) and several other proteins. Both Axin and APC are known to be critical for beta-catenin regulation, and truncations in APC that eliminate the Axin-binding site result in human cancers. A protease-resistant domain of Axin that contains the APC-binding site is a member of the regulators of G-protein signaling (RGS) superfamily. The crystal structures of this domain alone and in complex with an Axin-binding sequence from APC reveal that the Axin-APC interaction occurs at a conserved groove on a face of the protein that is distinct from the G-protein interface of classical RGS proteins. The molecular interactions observed in the Axin-APC complex provide a rationale for the evolutionary conservation seen in both proteins.

-	~~==Disease==~~	+	Structural basis of the Axin-adenomatous polyposis coli interaction.,Spink KE, Polakis P, Weis WI EMBO J. 2000 May 15;19(10):2270-9. PMID:10811618<ref>PMID:10811618</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma~~ (~~HCC~~) ~~[MIM~~:~~[http://omim~~.~~org/entry/114550 114550]].<ref>~~PMID:10700176</ref><ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[http://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:~~10700176~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~//www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; ~~down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos~~, ~~but also dorsalizes embryos by activating~~ a ~~Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation~~ of ~~CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates~~ the ~~phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation~~. ~~Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7~~. ~~Also component~~ of ~~the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development~~.<~~ref~~>~~PMID:12192039</ref><ref>PMID:16601693</ref><ref>PMID:17210684~~</~~ref~~>	+	</div>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~1dk8~~]] is a 1 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=1DK8 OCA].	+	*[[Axin\|Axin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:010811618</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Polakis, P.]]		[[Category: Polakis, P.]]

OCA at 21:26, 24 March 2013

OCA — Sun, 24 Mar 2013 21:26:36 GMT

←Older revision		Revision as of 21:26, 24 March 2013
Line 1:		Line 1:
-	[[Image:1dk8.png\|left\|200px]]
-
	{{STRUCTURE_1dk8\| PDB=1dk8 \| SCENE= }}		{{STRUCTURE_1dk8\| PDB=1dk8 \| SCENE= }}
-
	===CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN===		===CRYSTAL STRUCTURE OF THE RGS-HOMOLOGOUS DOMAIN OF AXIN===
		+	{{ABSTRACT_PUBMED_10811618}}

-	~~{{ABSTRACT_PUBMED_10811618}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[http://omim.org/entry/114550 114550]].<ref>PMID:10700176</ref><ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[http://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12192039</ref><ref>PMID:16601693</ref><ref>PMID:17210684</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010811618</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010811618</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Polakis, P.]]		[[Category: Polakis, P.]]

OCA: Protected "1dk8" [edit=sysop:move=sysop]

OCA — Wed, 31 Oct 2012 10:01:43 GMT

Protected "1dk8" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:01, 31 October 2012

←Older revision		Revision as of 09:27, 21 July 2021
Line 3:		Line 3:
	<StructureSection load='1dk8' size='340' side='right'caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>		<StructureSection load='1dk8' size='340' side='right'caption='[[1dk8]], [[Resolution\|resolution]] 1.57Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1dk8]] is a 1 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=1DK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DK8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1agr\|1agr]], [[1cmz\|1cmz]], [[1emu\|1emu]]</div></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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [~~http~~://pdbe.org/1dk8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1dk8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk8 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=1dk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk8 OCA], [https://pdbe.org/1dk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dk8 RCSB], [https://www.ebi.ac.uk/pdbsum/1dk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[~~http~~://omim.org/entry/114550 114550]].<ref>PMID:10700176</ref> <ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[~~http~~://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>	+	[[https://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Defects in AXIN1 are involved in hepatocellular carcinoma (HCC) [MIM:[https://omim.org/entry/114550 114550]].<ref>PMID:10700176</ref> <ref>PMID:12101426</ref> Defects in AXIN1 are a cause of caudal duplication anomaly (CADUA) [MIM:[https://omim.org/entry/607864 607864]]. Caudal duplication anomaly is characterized by the occurrence of duplications of different organs in the caudal region. Note=Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.<ref>PMID:10700176</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12192039</ref> <ref>PMID:16601693</ref> <ref>PMID:17210684</ref>	+	[[https://www.uniprot.org/uniprot/AXIN1_HUMAN AXIN1_HUMAN]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12192039</ref> <ref>PMID:16601693</ref> <ref>PMID:17210684</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]