3utm - Revision history

OCA at 14:08, 14 March 2024

2024-03-14T14:08:16Z

← Older revision		Revision as of 14:08, 14 March 2024
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	<StructureSection load='3utm' size='340' side='right'caption='[[3utm]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3utm' size='340' side='right'caption='[[3utm]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3utm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTM FirstGlance]. <br>		<table><tr><td colspan='2'>[[3utm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTM FirstGlance]. <br>
	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">TANKRYASE1, Tnks, Tnks1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Axin, Axin1, Fu ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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]] 2Å</td></tr>
	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~">~~<b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(+)_ADP~~-~~ribosyltransferase NAD(+) ADP-ribosyltransferase]~~, ~~with EC number~~ [~~https://www.brenda-enzymes.info/php/result_flat.php4?ecno=~~2~~.4.2.30 2.4.2.30] </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=3utm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utm OCA], [https://pdbe.org/3utm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3utm RCSB], [https://www.ebi.ac.uk/pdbsum/3utm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3utm 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=3utm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utm OCA], [https://pdbe.org/3utm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3utm RCSB], [https://www.ebi.ac.uk/pdbsum/3utm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3utm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/TNKS1_MOUSE TNKS1_MOUSE]] 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 (PARsylation) 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 PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1 (By similarity). [[https://www.uniprot.org/uniprot/AXIN1_MOUSE AXIN1_MOUSE]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). 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 (By similarity). Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12223491</ref> <ref>PMID:15526030</ref> <ref>PMID:17681137</ref>		[https://www.uniprot.org/uniprot/TNKS1_MOUSE TNKS1_MOUSE] 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 (PARsylation) 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 PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1 (By similarity).
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Axin is a tumor suppressor and a key negative regulator of the Wnt/beta-catenin signaling pathway. Axin turnover is controlled by its poly-ADP-ribosylation catalyzed by tankyrase (TNKS), which requires the direct interaction of Axin with TNKS. This interaction is thus an attractive drug target for treating cancers, brain injuries, and other diseases where beta-catenin is involved. Here we report the crystal structure of a mouse TNKS1 fragment containing ankyrin-repeat clusters 2 and 3 (ARC2-3) in a complex with the TNKS-binding domain of mouse Axin1. Surprisingly, we found that Axin contains two discrete TNKS-binding segments, both of which bind simultaneously to the two ARC2 domains in the ARC2-3 homodimer. Our crystal structure shows that in each TNKS-binding segment of Axin there is a conserved glycine residue that lies in the bottom of a narrow "gate" formed by two parallel tyrosine side chains on the TNKS surface. This glycine-selection gate is crucial for TNKS-Axin interactions, as mutation of the TNKS gate-forming residues, or mutation of either glycine residue in the two Axin segments, completely abolishes the binding of the corresponding Axin segment to TNKS. The bivalent binding of Axin to TNKS is required for Axin turnover, since mutations in either gate-binding glycine residue in Axin lead to Axin stabilization in the cell. In addition, our analyses also reveal the structural basis for TNKS substrate recruitment, and shed light on the overall structure of TNKS that should help in developing specific inhibitors of Wnt/beta-catenin signaling.

	Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment.,Morrone S, Cheng Z, Moon RT, Cong F, Xu W Proc Natl Acad Sci U S A. 2012 Jan 31;109(5):1500-5. Epub 2012 Jan 17. PMID:22307604<ref>PMID:22307604</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3utm" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Axin 3D structures\|Axin 3D structures]]		*[[Axin 3D structures\|Axin 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Mus musculus]]
	[[Category: Cheng, Z]]		[[Category: Cheng Z]]
	[[Category: Morrone, S]]		[[Category: Morrone S]]
	[[Category: Xu, W]]		[[Category: Xu W]]
	~~[[Category: Ankryin repeat cluster]]~~
	~~[[Category: Poly-adp-ribosylation]]~~
	~~[[Category: Tankyrase]]~~
	~~[[Category: Tnk]]~~
	~~[[Category: Transferase-signaling protein complex]]~~
	~~[[Category: Wnt signaling~~]]

OCA at 08:05, 20 July 2022

2022-07-20T08:05:50Z

← Older revision		Revision as of 08:05, 20 July 2022
Line 1:		Line 1:

	==Crystal structure of a mouse Tankyrase-Axin complex==		==Crystal structure of a mouse Tankyrase-Axin complex==
	<StructureSection load='3utm' size='340' side='right' caption='[[3utm]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3utm' size='340' side='right'caption='[[3utm]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3utm]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3UTM FirstGlance]. <br>		<table><tr><td colspan='2'>[[3utm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UTM FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TANKRYASE1, Tnks, Tnks1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Axin, Axin1, Fu ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TANKRYASE1, Tnks, Tnks1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Axin, Axin1, Fu ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </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=3utm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utm OCA], [~~http~~://pdbe.org/3utm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3utm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3utm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3utm 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=3utm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utm OCA], [https://pdbe.org/3utm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3utm RCSB], [https://www.ebi.ac.uk/pdbsum/3utm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3utm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/TNKS1_MOUSE TNKS1_MOUSE]] 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 (PARsylation) 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 PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1 (By similarity). [[~~http~~://www.uniprot.org/uniprot/AXIN1_MOUSE AXIN1_MOUSE]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). 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 (By similarity). Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12223491</ref> <ref>PMID:15526030</ref> <ref>PMID:17681137</ref>		[[https://www.uniprot.org/uniprot/TNKS1_MOUSE TNKS1_MOUSE]] 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 (PARsylation) 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 PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1 (By similarity). [[https://www.uniprot.org/uniprot/AXIN1_MOUSE AXIN1_MOUSE]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). 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 (By similarity). Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12223491</ref> <ref>PMID:15526030</ref> <ref>PMID:17681137</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
	*[[Axin\|Axin]]		*[[Axin 3D structures\|Axin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Cheng, Z]]		[[Category: Cheng, Z]]

OCA at 12:06, 4 August 2016

2016-08-04T12:06:42Z

← Older revision		Revision as of 12:06, 4 August 2016
Line 1:		Line 1:

	==Crystal structure of a mouse Tankyrase-Axin complex==		==Crystal structure of a mouse Tankyrase-Axin complex==
	<StructureSection load='3utm' size='340' side='right' caption='[[3utm]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3utm' size='340' side='right' caption='[[3utm]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3utm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTM FirstGlance]. <br>		<table><tr><td colspan='2'>[[3utm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTM FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TANKRYASE1, Tnks, Tnks1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~]), Axin, Axin1, Fu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TANKRYASE1, Tnks, Tnks1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Axin, Axin1, Fu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </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=3utm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3utm RCSB], [http://www.ebi.ac.uk/pdbsum/3utm 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=3utm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utm OCA], [http://pdbe.org/3utm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3utm RCSB], [http://www.ebi.ac.uk/pdbsum/3utm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3utm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 3utm" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Mus musculus~~]]		[[Category: Lk3 transgenic mice]]
	[[Category: Cheng, Z]]		[[Category: Cheng, Z]]
	[[Category: Morrone, S]]		[[Category: Morrone, S]]

OCA at 14:18, 24 December 2014

2014-12-24T14:18:00Z

← Older revision		Revision as of 14:18, 24 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3utm~~\| ~~PDB~~=3utm \| ~~SCENE~~= }}		==Crystal structure of a mouse Tankyrase-Axin complex==
	===~~Crystal structure~~ of a ~~mouse Tankyrase~~-~~Axin~~ complex===		<StructureSection load='3utm' size='340' side='right' caption='[[3utm]], [[Resolution\|resolution]] 2.00Å' scene=''>
	~~{{ABSTRACT_PUBMED_22307604}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3utm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTM FirstGlance]. <br>
			</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TANKRYASE1, Tnks, Tnks1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), Axin, Axin1, Fu ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </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=3utm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3utm RCSB], [http://www.ebi.ac.uk/pdbsum/3utm PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/TNKS1_MOUSE TNKS1_MOUSE]] 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 (PARsylation) 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 PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1 (By similarity). [[http://www.uniprot.org/uniprot/AXIN1_MOUSE AXIN1_MOUSE]] Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). 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 (By similarity). Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.<ref>PMID:12223491</ref> <ref>PMID:15526030</ref> <ref>PMID:17681137</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Axin is a tumor suppressor and a key negative regulator of the Wnt/beta-catenin signaling pathway. Axin turnover is controlled by its poly-ADP-ribosylation catalyzed by tankyrase (TNKS), which requires the direct interaction of Axin with TNKS. This interaction is thus an attractive drug target for treating cancers, brain injuries, and other diseases where beta-catenin is involved. Here we report the crystal structure of a mouse TNKS1 fragment containing ankyrin-repeat clusters 2 and 3 (ARC2-3) in a complex with the TNKS-binding domain of mouse Axin1. Surprisingly, we found that Axin contains two discrete TNKS-binding segments, both of which bind simultaneously to the two ARC2 domains in the ARC2-3 homodimer. Our crystal structure shows that in each TNKS-binding segment of Axin there is a conserved glycine residue that lies in the bottom of a narrow "gate" formed by two parallel tyrosine side chains on the TNKS surface. This glycine-selection gate is crucial for TNKS-Axin interactions, as mutation of the TNKS gate-forming residues, or mutation of either glycine residue in the two Axin segments, completely abolishes the binding of the corresponding Axin segment to TNKS. The bivalent binding of Axin to TNKS is required for Axin turnover, since mutations in either gate-binding glycine residue in Axin lead to Axin stabilization in the cell. In addition, our analyses also reveal the structural basis for TNKS substrate recruitment, and shed light on the overall structure of TNKS that should help in developing specific inhibitors of Wnt/beta-catenin signaling.

	~~==About this Structure==~~		Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment.,Morrone S, Cheng Z, Moon RT, Cong F, Xu W Proc Natl Acad Sci U S A. 2012 Jan 31;109(5):1500-5. Epub 2012 Jan 17. PMID:22307604<ref>PMID:22307604</ref>
	~~[[3utm]] is~~ a ~~3 chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3UTM OCA].~~
			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	==See Also==		==See Also==
	*[[Axin\|Axin]]		*[[Axin\|Axin]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:022307604<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Cheng, Z.]]		[[Category: Cheng, Z]]
	[[Category: Morrone, S.]]		[[Category: Morrone, S]]
	[[Category: Xu, W.]]		[[Category: Xu, W]]
	[[Category: Ankryin repeat cluster]]		[[Category: Ankryin repeat cluster]]
	[[Category: Poly-adp-ribosylation]]		[[Category: Poly-adp-ribosylation]]

OCA at 09:07, 11 March 2013

2013-03-11T09:07:48Z

← Older revision		Revision as of 09:07, 11 March 2013
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	~~[[Image:3utm.png\|left\|200px]]~~

	{{STRUCTURE_3utm\| PDB=3utm \| SCENE= }}		{{STRUCTURE_3utm\| PDB=3utm \| SCENE= }}

	===Crystal structure of a mouse Tankyrase-Axin complex===		===Crystal structure of a mouse Tankyrase-Axin complex===

	{{ABSTRACT_PUBMED_22307604}}		{{ABSTRACT_PUBMED_22307604}}

OCA at 06:19, 20 October 2012

2012-10-20T06:19:45Z

← Older revision		Revision as of 06:19, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[3utm]] is a 3 chain structure ~~of [[Axin]]~~ with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA].		[[3utm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA].

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

OCA at 12:49, 25 July 2012

2012-07-25T12:49:37Z

← Older revision		Revision as of 12:49, 25 July 2012
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	[[Image:3utm.png\|left\|200px]]		[[Image:3utm.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3utm", 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_3utm\| PDB=3utm \| SCENE= }}		{{STRUCTURE_3utm\| PDB=3utm \| SCENE= }}

	===Crystal structure of a mouse Tankyrase-Axin complex===		===Crystal structure of a mouse Tankyrase-Axin complex===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_22307604}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 22307604 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_22307604}}		{{ABSTRACT_PUBMED_22307604}}

	==About this Structure==		==About this Structure==
	[[3utm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA].		[[3utm]] is a 3 chain structure of [[Axin]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA].

			==See Also==
			*[[Axin\|Axin]]

	==Reference==		==Reference==

OCA at 08:44, 29 February 2012

2012-02-29T08:44:10Z

← Older revision		Revision as of 08:44, 29 February 2012
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	===Crystal structure of a mouse Tankyrase-Axin complex===		===Crystal structure of a mouse Tankyrase-Axin complex===


			<!--
			The line below this paragraph, {{ABSTRACT_PUBMED_22307604}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 22307604 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_22307604}}

	==About this Structure==		==About this Structure==

OCA at 06:34, 22 February 2012

2012-02-22T06:34:39Z

← Older revision		Revision as of 06:34, 22 February 2012
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	[[Image:3utm.~~jpg~~\|left\|200px]]		[[Image:3utm.png\|left\|200px]]

	<!--		<!--
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	==About this Structure==		==About this Structure==
	[[3utm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA].		[[3utm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTM OCA].

			==Reference==
			<ref group="xtra">PMID:022307604</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Cheng, Z.]]		[[Category: Cheng, Z.]]

OCA at 10:54, 18 January 2012

2012-01-18T10:54:08Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:3utm.jpg|left|200px]]
-The entry 3utm is ON HOLD  until Paper Publication
+<!--
-Authors: Cheng, Z., Morrone, S., Xu, W.
+===Crystal structure of a mouse Tankyrase-Axin complex===
-Description: Crystal structure of a mouse Tankyrase-Axin complex