3m0a - Revision history

OCA at 10:23, 21 February 2024

OCA — Wed, 21 Feb 2024 10:23:19 GMT

←Older revision		Revision as of 10:23, 21 February 2024
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	==Crystal structure of TRAF2:cIAP2 complex==		==Crystal structure of TRAF2:cIAP2 complex==
-	<StructureSection load='3m0a' size='340' side='right' caption='[[3m0a]], [[Resolution\|resolution]] 2.61Å' scene=''>	+	<StructureSection load='3m0a' size='340' side='right'caption='[[3m0a]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m0a]] is a 4 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=3M0A OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3M0A FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m0a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M0A FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><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]] 2.61Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m06\|3m06]]~~, [[~~3m0d~~\|~~3m0d~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~TRAF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=9606 HUMAN]), BIRC3, API2, IAP1, MIHC, RNF49 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=3m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0a OCA], [https://pdbe.org/3m0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m0a RCSB], [https://www.ebi.ac.uk/pdbsum/3m0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m0a ProSAT]</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=3m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0a OCA], [~~http~~://pdbe.org/3m0a PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3m0a RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3m0a PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3m0a ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Note=A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref> <ref>PMID:11907583</ref> <ref>PMID:12917689</ref> <ref>PMID:15383523</ref> <ref>PMID:19506082</ref> <ref>PMID:19150425</ref> <ref>PMID:18981220</ref> <ref>PMID:19918265</ref> <ref>PMID:20064526</ref> <ref>PMID:19937093</ref> <ref>PMID:20047764</ref> <ref>PMID:20577214</ref> <ref>PMID:19810754</ref> <ref>PMID:20385093</ref> [[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.<ref>PMID:21931591</ref>	+	[https://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref> <ref>PMID:11907583</ref> <ref>PMID:12917689</ref> <ref>PMID:15383523</ref> <ref>PMID:19506082</ref> <ref>PMID:19150425</ref> <ref>PMID:18981220</ref> <ref>PMID:19918265</ref> <ref>PMID:20064526</ref> <ref>PMID:19937093</ref> <ref>PMID:20047764</ref> <ref>PMID:20577214</ref> <ref>PMID:19810754</ref> <ref>PMID:20385093</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m0/3m0a_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m0/3m0a_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>
Line 23:		Line 20:
	</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=3m0a 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=3m0a ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	TRAF1/2 and cIAP1/2 are members of the TNF receptor-associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for canonical and noncanonical NF-kappaB signaling pathways. Here, we report the crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes. A TRAF2 trimer interacts with one cIAP2 both in the crystal and in solution. Two chains of the TRAF2 trimer directly contact cIAP2, and key residues at the interface are confirmed by mutagenesis. TRAF1 and TRAF2 preferentially form the TRAF1: (TRAF2)(2) heterotrimer, which interacts with cIAP2 more strongly than TRAF2 alone. In contrast, TRAF1 alone interacts very weakly with cIAP2. Surprisingly, TRAF1 and one chain of TRAF2 in the TRAF1: (TRAF2)(2): cIAP2 ternary complex mediate interaction with cIAP2. Because TRAF1 is upregulated by many stimuli, it may modulate the interaction of TRAF2 with cIAP1/2, which explains regulatory roles of TRAF1 in TNF signaling.
-
-	Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.,Zheng C, Kabaleeswaran V, Wang Y, Cheng G, Wu H Mol Cell. 2010 Apr 9;38(1):101-13. PMID:20385093<ref>PMID:20385093</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3m0a" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Baculoviral IAP repeat-containing protein\|Baculoviral IAP repeat-containing protein]]	+	*[[TNF receptor-associated factor 3D structures\|TNF receptor-associated factor 3D structures]]
-	*[[TNF receptor-associated factor\|TNF receptor-associated factor]]	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Kabaleeswaran, V~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Wu, H~~]]	+	[[Category: Kabaleeswaran V]]
-	[[Category: ~~Apoptosis]]~~	+	[[Category: Wu H]]
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Traf2: ciap2 and the traf1: traf2: ciap2 complex~~]]	+

OCA at 13:30, 4 May 2017

OCA — Thu, 04 May 2017 13:30:51 GMT

←Older revision		Revision as of 13:30, 4 May 2017
Line 1:		Line 1:
		+
	==Crystal structure of TRAF2:cIAP2 complex==		==Crystal structure of TRAF2:cIAP2 complex==
	<StructureSection load='3m0a' size='340' side='right' caption='[[3m0a]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='3m0a' size='340' side='right' caption='[[3m0a]], [[Resolution\|resolution]] 2.61Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m06\|3m06]], [[3m0d\|3m0d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m06\|3m06]], [[3m0d\|3m0d]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRAF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BIRC3, API2, IAP1, MIHC, RNF49 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRAF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BIRC3, API2, IAP1, MIHC, RNF49 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0a RCSB], [http://www.ebi.ac.uk/pdbsum/3m0a 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=3m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0a OCA], [http://pdbe.org/3m0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m0a RCSB], [http://www.ebi.ac.uk/pdbsum/3m0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m0a ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	<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=3m0a ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 31:
	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 3m0a" style="background-color:#fffaf0;"></div>

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

OCA at 08:33, 29 July 2015

OCA — Wed, 29 Jul 2015 08:33:38 GMT

←Older revision		Revision as of 08:33, 29 July 2015
Line 2:		Line 2:
	<StructureSection load='3m0a' size='340' side='right' caption='[[3m0a]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='3m0a' size='340' side='right' caption='[[3m0a]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m0a]] is a 4 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=3M0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M0A FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m0a]] is a 4 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=3M0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M0A FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m06\|3m06]], [[3m0d\|3m0d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m06\|3m06]], [[3m0d\|3m0d]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRAF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), BIRC3, API2, IAP1, MIHC, RNF49 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRAF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BIRC3, API2, IAP1, MIHC, RNF49 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0a RCSB], [http://www.ebi.ac.uk/pdbsum/3m0a 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=3m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0a RCSB], [http://www.ebi.ac.uk/pdbsum/3m0a PDBsum]</span></td></tr>
	</table>		</table>
Line 30:		Line 30:
	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>
		+
		+	==See Also==
		+	*[[Baculoviral IAP repeat-containing protein\|Baculoviral IAP repeat-containing protein]]
		+	*[[TNF receptor-associated factor\|TNF receptor-associated factor]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Kabaleeswaran, V]]		[[Category: Kabaleeswaran, V]]
	[[Category: Wu, H]]		[[Category: Wu, H]]

OCA at 16:07, 18 December 2014

OCA — Thu, 18 Dec 2014 16:07:37 GMT

←Older revision		Revision as of 16:07, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3m0a\| PDB~~=3m0a \| ~~SCENE~~= }}	+	==Crystal structure of TRAF2:cIAP2 complex==
-	===~~Crystal~~ structure of TRAF2:~~cIAP2 complex~~===	+	<StructureSection load='3m0a' size='340' side='right' caption='[[3m0a]], [[Resolution\|resolution]] 2.61Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20385093}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3m0a]] is a 4 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=3M0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M0A FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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">[[3m06\|3m06]], [[3m0d\|3m0d]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRAF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BIRC3, API2, IAP1, MIHC, RNF49 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m0a RCSB], [http://www.ebi.ac.uk/pdbsum/3m0a PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Note=A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.		[[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Note=A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref> <ref>PMID:11907583</ref> <ref>PMID:12917689</ref> <ref>PMID:15383523</ref> <ref>PMID:19506082</ref> <ref>PMID:19150425</ref> <ref>PMID:18981220</ref> <ref>PMID:19918265</ref> <ref>PMID:20064526</ref> <ref>PMID:19937093</ref> <ref>PMID:20047764</ref> <ref>PMID:20577214</ref> <ref>PMID:19810754</ref> <ref>PMID:20385093</ref> [[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.<ref>PMID:21931591</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/m0/3m0a_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 ==
		+	TRAF1/2 and cIAP1/2 are members of the TNF receptor-associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for canonical and noncanonical NF-kappaB signaling pathways. Here, we report the crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes. A TRAF2 trimer interacts with one cIAP2 both in the crystal and in solution. Two chains of the TRAF2 trimer directly contact cIAP2, and key residues at the interface are confirmed by mutagenesis. TRAF1 and TRAF2 preferentially form the TRAF1: (TRAF2)(2) heterotrimer, which interacts with cIAP2 more strongly than TRAF2 alone. In contrast, TRAF1 alone interacts very weakly with cIAP2. Surprisingly, TRAF1 and one chain of TRAF2 in the TRAF1: (TRAF2)(2): cIAP2 ternary complex mediate interaction with cIAP2. Because TRAF1 is upregulated by many stimuli, it may modulate the interaction of TRAF2 with cIAP1/2, which explains regulatory roles of TRAF1 in TNF signaling.

-	~~==Function==~~	+	Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.,Zheng C, Kabaleeswaran V, Wang Y, Cheng G, Wu H Mol Cell. 2010 Apr 9;38(1):101-13. PMID:20385093<ref>PMID:20385093</ref>
-	~~[[http://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation~~ of ~~NF-kappa-B and JNK and plays a central role in~~ the ~~regulation of cell survival~~ and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 ~~RING-type zinc finger domain.<ref>PMID~~:~~10346818</ref><ref>PMID~~:11907583</ref><ref>PMID:12917689</ref><ref>PMID:15383523</ref><ref>PMID:19506082</ref><ref>PMID:19150425</ref><ref>PMID:18981220</ref><ref>PMID:19918265</ref><ref>PMID:20064526</ref><ref>PMID:19937093</ref><ref>PMID:20047764</ref><ref>PMID:20577214</ref><ref>PMID:19810754</ref><ref>PMID:20385093</ref> [[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Multi-functional protein which regulates not only caspases and apoptosis, ~~but also modulates inflammatory signaling and immunity~~, ~~mitogenic kinase signaling~~ and ~~cell proliferation, as well as cell invasion and metastasis~~. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, ~~RIPK2~~, ~~RIPK3~~, ~~RIPK4~~, ~~CASP3~~, ~~CASP7, CASP8, TRAF1, and BCL10~~. ~~Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors~~ (~~TLRs~~)~~, Nodlike receptors (NLRs) and RIG~~-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.<ref>PMID:~~21931591~~</ref>	+
-		+
-	~~==About this Structure==~~	+
-	[[3m0a]] is a 4 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=3M0A OCA].	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:020385093</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Kabaleeswaran, V.]]	+	[[Category: Kabaleeswaran, V]]
-	[[Category: Wu, H.]]	+	[[Category: Wu, H]]
	[[Category: Apoptosis]]		[[Category: Apoptosis]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]

OCA: Protected "3m0a" [edit=sysop:move=sysop]

OCA — Mon, 25 Mar 2013 00:17:32 GMT

Protected "3m0a" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:17, 25 March 2013

OCA at 00:17, 25 March 2013

OCA — Mon, 25 Mar 2013 00:17:30 GMT

←Older revision		Revision as of 00:17, 25 March 2013
Line 1:		Line 1:
-	{{Seed}}
-	[[Image:3m0a.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3m0a", 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_3m0a\| PDB=3m0a \| SCENE= }}		{{STRUCTURE_3m0a\| PDB=3m0a \| SCENE= }}
-
	===Crystal structure of TRAF2:cIAP2 complex===		===Crystal structure of TRAF2:cIAP2 complex===
		+	{{ABSTRACT_PUBMED_20385093}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Note=A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.

-	<!--	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_20385093}}, adds~~ the ~~Publication Abstract~~ to ~~the page~~	+	[[http://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref><ref>PMID:11907583</ref><ref>PMID:12917689</ref><ref>PMID:15383523</ref><ref>PMID:19506082</ref><ref>PMID:19150425</ref><ref>PMID:18981220</ref><ref>PMID:19918265</ref><ref>PMID:20064526</ref><ref>PMID:19937093</ref><ref>PMID:20047764</ref><ref>PMID:20577214</ref><ref>PMID:19810754</ref><ref>PMID:20385093</ref> [[http://www.uniprot.org/uniprot/BIRC3_HUMAN BIRC3_HUMAN]] Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.<ref>PMID:21931591</ref>
-	(as it ~~appears~~ on ~~PubMed at~~ http://www.~~pubmed~~.~~gov)~~, ~~where 20385093 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_20385093}}~~	+

	==About this Structure==		==About this Structure==
-	~~3M0A~~ is a 4 ~~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=3M0A OCA].	+	[[3m0a]] is a 4 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=3M0A OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20385093~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020385093</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Kabaleeswaran, V.]]		[[Category: Kabaleeswaran, V.]]
	[[Category: Wu, H.]]		[[Category: Wu, H.]]
	[[Category: Apoptosis]]		[[Category: Apoptosis]]
-	[[Category: Coiled coil]]
-	[[Category: Cytoplasm]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-	[[Category: Polymorphism]]
	[[Category: Signaling protein]]		[[Category: Signaling protein]]
	[[Category: Traf2: ciap2 and the traf1: traf2: ciap2 complex]]		[[Category: Traf2: ciap2 and the traf1: traf2: ciap2 complex]]
-	[[Category: Ubl conjugation]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 28 10:56:13 2010''

OCA at 07:56, 28 April 2010

OCA — Wed, 28 Apr 2010 07:56:14 GMT

←Older revision		Revision as of 07:56, 28 April 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3m0a.jpg\|left\|200px]]

-	The ~~entry 3m0a~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3m0a", 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_3m0a\| PDB=3m0a \| SCENE= }}

-	~~Authors~~: ~~Kabaleeswaran, V., Wu, H.~~	+	===Crystal structure of TRAF2:cIAP2 complex===

-	Description: Crystal structure of TRAF2:cIAP2 complex

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr ~~14 09~~:21:11 2010''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20385093}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20385093 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20385093}}
		+
		+	==About this Structure==
		+	3M0A is a 4 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=3M0A OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20385093</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Kabaleeswaran, V.]]
		+	[[Category: Wu, H.]]
		+	[[Category: Apoptosis]]
		+	[[Category: Coiled coil]]
		+	[[Category: Cytoplasm]]
		+	[[Category: Metal-binding]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Polymorphism]]
		+	[[Category: Signaling protein]]
		+	[[Category: Traf2: ciap2 and the traf1: traf2: ciap2 complex]]
		+	[[Category: Ubl conjugation]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 28 10:56:13 2010''

OCA at 06:21, 14 April 2010

OCA — Wed, 14 Apr 2010 06:21:12 GMT

←Older revision		Revision as of 06:21, 14 April 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3m0a is ON HOLD	+	The entry 3m0a is ON HOLD until Paper Publication

	Authors: Kabaleeswaran, V., Wu, H.		Authors: Kabaleeswaran, V., Wu, H.
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	Description: Crystal structure of TRAF2:cIAP2 complex		Description: Crystal structure of TRAF2:cIAP2 complex

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Mar 17~~ 09:12:24 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 14 09:21:11 2010''

OCA at 07:12, 17 March 2010

OCA — Wed, 17 Mar 2010 07:12:24 GMT

←Older revision		Revision as of 07:12, 17 March 2010
Line 3:		Line 3:
	The entry 3m0a is ON HOLD		The entry 3m0a is ON HOLD

-	Authors: ~~Venkataraman,~~ Kabaleeswaran, ~~Hao~~, wu	+	Authors: Kabaleeswaran, V., Wu, H.

	Description: Crystal structure of TRAF2:cIAP2 complex		Description: Crystal structure of TRAF2:cIAP2 complex

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar ~~10 13:~~17:56 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 17 09:12:24 2010''

OCA: New page: '''Unreleased structure''' The entry 3m0a is ON HOLD Authors: Venkataraman, Kabaleeswaran, Hao, wu Description: Crystal structure of TRAF2:cIAP2 complex ''Page seeded by [http://oca.w...

OCA — Wed, 10 Mar 2010 11:17:57 GMT

New page: '''Unreleased structure''' The entry 3m0a is ON HOLD Authors: Venkataraman, Kabaleeswaran, Hao, wu Description: Crystal structure of TRAF2:cIAP2 complex ''Page seeded by [http://oca.w...

New page

'''Unreleased structure'''

The entry 3m0a is ON HOLD

Authors: Venkataraman, Kabaleeswaran, Hao, wu

Description: Crystal structure of TRAF2:cIAP2 complex

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 10 13:17:56 2010''