4dbg - Revision history

OCA at 08:10, 21 September 2022

2022-09-21T08:10:05Z

←Older revision		Revision as of 08:10, 21 September 2022
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	==Crystal structure of HOIL-1L-UBL complexed with a HOIP-UBA derivative==		==Crystal structure of HOIL-1L-UBL complexed with a HOIP-UBA derivative==
-	<StructureSection load='4dbg' size='340' side='right' caption='[[4dbg]], [[Resolution\|resolution]] 2.71Å' scene=''>	+	<StructureSection load='4dbg' size='340' side='right'caption='[[4dbg]], [[Resolution\|resolution]] 2.71Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dbg]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DBG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dbg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DBG FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBCK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RNF31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</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=4dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbg OCA], [https://pdbe.org/4dbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dbg RCSB], [https://www.ebi.ac.uk/pdbsum/4dbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbg 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=4dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbg OCA], [~~http~~://pdbe.org/4dbg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dbg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dbg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbg ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.	+	[[https://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.<ref>PMID:12629548</ref> <ref>PMID:17006537</ref> <ref>PMID:17449468</ref> <ref>PMID:18711448</ref> <ref>PMID:20005846</ref> <ref>PMID:19136968</ref> <ref>PMID:21455173</ref> <ref>PMID:21455180</ref> <ref>PMID:21455181</ref> [[http://www.uniprot.org/uniprot/RNF31_HUMAN RNF31_HUMAN]] E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('M-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Binds polyubiquitin of different linkage types.<ref>PMID:17006537</ref> <ref>PMID:20005846</ref> <ref>PMID:19136968</ref> <ref>PMID:21455173</ref> <ref>PMID:21455180</ref> <ref>PMID:21455181</ref> <ref>PMID:22863777</ref>	+	[[https://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.<ref>PMID:12629548</ref> <ref>PMID:17006537</ref> <ref>PMID:17449468</ref> <ref>PMID:18711448</ref> <ref>PMID:20005846</ref> <ref>PMID:19136968</ref> <ref>PMID:21455173</ref> <ref>PMID:21455180</ref> <ref>PMID:21455181</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Hiromoto, T]]	+	[[Category: Large Structures]]
-	[[Category: Kato, K]]	+	[[Category: Hiromoto T]]
-	[[Category: Kurimoto, E]]	+	[[Category: Kato K]]
-	[[Category: Mizushima, T]]	+	[[Category: Kurimoto E]]
-	[[Category: Yagi, H]]	+	[[Category: Mizushima T]]
-	~~[[Category: Ligase]]~~	+	[[Category: Yagi H]]
-	~~[[Category: Ubiquitin fold]]~~	+
-	~~[[Category: Ubiquitination~~]]	+

OCA at 13:35, 11 August 2016

2016-08-11T13:35:49Z

←Older revision		Revision as of 13:35, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of HOIL-1L-UBL complexed with a HOIP-UBA derivative==		==Crystal structure of HOIL-1L-UBL complexed with a HOIP-UBA derivative==
	<StructureSection load='4dbg' size='340' side='right' caption='[[4dbg]], [[Resolution\|resolution]] 2.71Å' scene=''>		<StructureSection load='4dbg' size='340' side='right' caption='[[4dbg]], [[Resolution\|resolution]] 2.71Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBG FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBCK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), RNF31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBCK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RNF31 ([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=4dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dbg RCSB], [http://www.ebi.ac.uk/pdbsum/4dbg 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=4dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbg OCA], [http://pdbe.org/4dbg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dbg RCSB], [http://www.ebi.ac.uk/pdbsum/4dbg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbg ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	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 4dbg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hiromoto, T]]		[[Category: Hiromoto, T]]
	[[Category: Kato, K]]		[[Category: Kato, K]]

OCA at 13:55, 4 January 2015

2015-01-04T13:55:13Z

←Older revision		Revision as of 13:55, 4 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4dbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4dbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBCK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RNF31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBCK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RNF31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dbg RCSB], [http://www.ebi.ac.uk/pdbsum/4dbg 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=4dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dbg RCSB], [http://www.ebi.ac.uk/pdbsum/4dbg PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.		[[http://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Hiromoto, T.]]	+	[[Category: Hiromoto, T]]
-	[[Category: Kato, K.]]	+	[[Category: Kato, K]]
-	[[Category: Kurimoto, E.]]	+	[[Category: Kurimoto, E]]
-	[[Category: Mizushima, T.]]	+	[[Category: Mizushima, T]]
-	[[Category: Yagi, H.]]	+	[[Category: Yagi, H]]
	[[Category: Ligase]]		[[Category: Ligase]]
	[[Category: Ubiquitin fold]]		[[Category: Ubiquitin fold]]
	[[Category: Ubiquitination]]		[[Category: Ubiquitination]]

OCA at 07:37, 5 June 2014

2014-06-05T07:37:55Z

←Older revision		Revision as of 07:37, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~4dbg.~~png~~\|~~left\|200px~~]]	+	==Crystal structure of HOIL-1L-UBL complexed with a HOIP-UBA derivative==
		+	<StructureSection load='4dbg' size='340' side='right' caption='[[4dbg]], [[Resolution\|resolution]] 2.71Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4dbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RBCK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RNF31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4dbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dbg RCSB], [http://www.ebi.ac.uk/pdbsum/4dbg PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HOIL1_HUMAN HOIL1_HUMAN]] E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.<ref>PMID:12629548</ref> <ref>PMID:17006537</ref> <ref>PMID:17449468</ref> <ref>PMID:18711448</ref> <ref>PMID:20005846</ref> <ref>PMID:19136968</ref> <ref>PMID:21455173</ref> <ref>PMID:21455180</ref> <ref>PMID:21455181</ref> [[http://www.uniprot.org/uniprot/RNF31_HUMAN RNF31_HUMAN]] E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('M-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Binds polyubiquitin of different linkage types.<ref>PMID:17006537</ref> <ref>PMID:20005846</ref> <ref>PMID:19136968</ref> <ref>PMID:21455173</ref> <ref>PMID:21455180</ref> <ref>PMID:21455181</ref> <ref>PMID:22863777</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-kappaB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-kappaB activation. This study highlights the versatility and specificity of protein-protein interactions involving Ub/UBLs and their cognate proteins.

-	<!--	+	A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex.,Yagi H, Ishimoto K, Hiromoto T, Fujita H, Mizushima T, Uekusa Y, Yagi-Utsumi M, Kurimoto E, Noda M, Uchiyama S, Tokunaga F, Iwai K, Kato K EMBO Rep. 2012 Mar 20. doi: 10.1038/embor.2012.24. PMID:22430200<ref>PMID:22430200</ref>
-	~~The line below this paragraph, containing "STRUCTURE_4dbg", 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_4dbg\| PDB=4dbg \| SCENE= }}~~	+

-	~~===Crystal structure~~ of ~~HOIL-1L-UBL complexed with a HOIP-UBA derivative===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22430200}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 22430200 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_22430200}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[4dbg]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022430200<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hiromoto, T.]]		[[Category: Hiromoto, T.]]

OCA at 06:10, 11 April 2012

2012-04-11T06:10:11Z

←Older revision		Revision as of 06:10, 11 April 2012
Line 1:		Line 1:
-	[[Image:4dbg.~~jpg~~\|left\|200px]]	+	[[Image:4dbg.png\|left\|200px]]

	<!--		<!--
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-	===Crystal structure of HOIL-1L-UBL complexed with HOIP-UBA derivative===	+	===Crystal structure of HOIL-1L-UBL complexed with a HOIP-UBA derivative===

OCA at 06:06, 4 April 2012

2012-04-04T06:06:39Z

←Older revision		Revision as of 06:06, 4 April 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4dbg.jpg\|left\|200px]]

-	The ~~entry 4dbg~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_4dbg", 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_4dbg\| PDB=4dbg \| SCENE= }}

-	~~Authors: Yagi, H., Hiromoto, T., Mizushima, T., Kurimoto, E., Kato, K.~~	+	===Crystal structure of HOIL-1L-UBL complexed with HOIP-UBA derivative===

-	~~Description~~: ~~Crystal~~ Structure of a ~~UBL~~-~~UBA Complex~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22430200}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22430200 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22430200}}
		+
		+	==About this Structure==
		+	[[4dbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBG OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022430200</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Hiromoto, T.]]
		+	[[Category: Kato, K.]]
		+	[[Category: Kurimoto, E.]]
		+	[[Category: Mizushima, T.]]
		+	[[Category: Yagi, H.]]
		+	[[Category: Ligase]]
		+	[[Category: Ubiquitin fold]]
		+	[[Category: Ubiquitination]]

OCA at 06:59, 1 February 2012

2012-02-01T06:59:39Z

←Older revision		Revision as of 06:59, 1 February 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4dbg is ON HOLD	+	The entry 4dbg is ON HOLD until Paper Publication

	Authors: Yagi, H., Hiromoto, T., Mizushima, T., Kurimoto, E., Kato, K.		Authors: Yagi, H., Hiromoto, T., Mizushima, T., Kurimoto, E., Kato, K.

	Description: Crystal Structure of a UBL-UBA Complex		Description: Crystal Structure of a UBL-UBA Complex

OCA: Protected "4dbg" [edit=sysop:move=sysop]

2012-01-25T06:10:33Z

Protected "4dbg" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:10, 25 January 2012

OCA: New page: '''Unreleased structure''' The entry 4dbg is ON HOLD Authors: Yagi, H., Hiromoto, T., Mizushima, T., Kurimoto, E., Kato, K. Description: Crystal Structure of a UBL-UBA Complex

2012-01-25T06:10:32Z

New page: '''Unreleased structure''' The entry 4dbg is ON HOLD Authors: Yagi, H., Hiromoto, T., Mizushima, T., Kurimoto, E., Kato, K. Description: Crystal Structure of a UBL-UBA Complex

New page

'''Unreleased structure'''

The entry 4dbg is ON HOLD

Authors: Yagi, H., Hiromoto, T., Mizushima, T., Kurimoto, E., Kato, K.

Description: Crystal Structure of a UBL-UBA Complex