2fun - Revision history

OCA at 09:32, 30 August 2023

2023-08-30T09:32:05Z

← Older revision		Revision as of 09:32, 30 August 2023
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	<StructureSection load='2fun' size='340' side='right'caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='2fun' size='340' side='right'caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Acmnpv Acmnpv~~] and [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FUN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FUN FirstGlance]. <br>
	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1i4e\|1i4e]]</div></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]] 3Å</td></tr>
	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">P35 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=46015 AcMNPV])~~</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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [https://pdbe.org/2fun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [https://www.ebi.ac.uk/pdbsum/2fun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fun 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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [https://pdbe.org/2fun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [https://www.ebi.ac.uk/pdbsum/2fun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fun ProSAT]</span></td></tr>
	</table>		</table>
	~~== Disease ==~~
	[[https://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:[https://omim.org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.<ref>PMID:12353035</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/~~VP35_NPVAC VP35_NPVAC~~]~~] Blocks~~ the insect ~~or worm~~ host ~~cells~~ apoptotic response initiated by the viral infection. ~~Confers protection from cell death in mammalian cells. Acts by blocking~~ the activity of members of the caspase family of proteases. Required for late and very late gene expression. ~~[[https~~://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-\|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.<ref>PMID:~~12010809~~</ref> <ref>PMID:~~9006941~~</ref>		[https://www.uniprot.org/uniprot/P35_NPVAC P35_NPVAC] Functions as an inhibitor of the host RNA interference antiviral response. Inhibits the insect host cell apoptotic response initiated by the viral infection. Blocks as well the activity of members of the caspase family of proteases. Required for late and very late gene expression.<ref>PMID:16081248</ref> <ref>PMID:1962198</ref> <ref>PMID:26018163</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Acmnpv~~]]		[[Category: Autographa californica nucleopolyhedrovirus]]
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Eliezer, D]]		[[Category: Eliezer D]]
	[[Category: Lu, M]]		[[Category: Lu M]]
	[[Category: Min, T]]		[[Category: Min T]]
	[[Category: Wu, H]]		[[Category: Wu H]]
	~~[[Category: Apoptosis-hydrolase complex]]~~
	~~[[Category: Apoptosis/hydrolase~~]]

OCA at 15:33, 3 March 2021

2021-03-03T15:33:44Z

← Older revision		Revision as of 15:33, 3 March 2021
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	==alternative p35-caspase-8 complex==		==alternative p35-caspase-8 complex==
	<StructureSection load='2fun' size='340' side='right' caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='2fun' size='340' side='right'caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Acmnpv Acmnpv] and [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2FUN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acmnpv Acmnpv] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FUN FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i4e\|1i4e]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 AcMNPV])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 AcMNPV])</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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [~~http~~://pdbe.org/2fun PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2fun PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2fun 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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [https://pdbe.org/2fun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [https://www.ebi.ac.uk/pdbsum/2fun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fun ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:[~~http~~://omim.org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.<ref>PMID:12353035</ref>		[[https://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:[https://omim.org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.<ref>PMID:12353035</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/VP35_NPVAC VP35_NPVAC]] Blocks the insect or worm host cells apoptotic response initiated by the viral infection. Confers protection from cell death in mammalian cells. Acts by blocking the activity of members of the caspase family of proteases. Required for late and very late gene expression. [[~~http~~://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-\|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.<ref>PMID:12010809</ref> <ref>PMID:9006941</ref>		[[https://www.uniprot.org/uniprot/VP35_NPVAC VP35_NPVAC]] Blocks the insect or worm host cells apoptotic response initiated by the viral infection. Confers protection from cell death in mammalian cells. Acts by blocking the activity of members of the caspase family of proteases. Required for late and very late gene expression. [[https://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-\|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.<ref>PMID:12010809</ref> <ref>PMID:9006941</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Caspase\|Caspase]]		*[[Caspase 3D structures\|Caspase 3D structures]]
	*[[User:Christopher French\|User:Christopher French]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Acmnpv]]		[[Category: Acmnpv]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Eliezer, D]]		[[Category: Eliezer, D]]
	[[Category: Lu, M]]		[[Category: Lu, M]]

OCA at 07:02, 20 June 2018

2018-06-20T07:02:47Z

← Older revision		Revision as of 07:02, 20 June 2018
Line 1:		Line 1:

	==alternative p35-caspase-8 complex==		==alternative p35-caspase-8 complex==
	<StructureSection load='2fun' size='340' side='right' caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='2fun' size='340' side='right' caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 AcMNPV])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 AcMNPV])</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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [http://pdbe.org/2fun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [http://www.ebi.ac.uk/pdbsum/2fun 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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [http://pdbe.org/2fun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [http://www.ebi.ac.uk/pdbsum/2fun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fun ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fu/2fun_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fu/2fun_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 04:45, 7 February 2016

2016-02-07T04:45:23Z

← Older revision		Revision as of 04:45, 7 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fun ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:58, 9 September 2015

2015-09-09T21:58:15Z

← Older revision		Revision as of 21:58, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='2fun' size='340' side='right' caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='2fun' size='340' side='right' caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus~~] and [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Acmnpv Acmnpv] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUN FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 ~~Autographa californica nucleopolyhedrovirus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 AcMNPV])</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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [http://www.ebi.ac.uk/pdbsum/2fun 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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [http://pdbe.org/2fun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [http://www.ebi.ac.uk/pdbsum/2fun PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 29:		Line 29:
	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 2fun" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Autographa californica nucleopolyhedrovirus~~]]		[[Category: Acmnpv]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Eliezer, D]]		[[Category: Eliezer, D]]
	[[Category: Lu, M]]		[[Category: Lu, M]]

OCA at 09:07, 16 January 2015

2015-01-16T09:07:05Z

← Older revision		Revision as of 09:07, 16 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUN FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 Autographa californica nucleopolyhedrovirus])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 Autographa californica nucleopolyhedrovirus])</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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [http://www.ebi.ac.uk/pdbsum/2fun 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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [http://www.ebi.ac.uk/pdbsum/2fun PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:[http://omim.org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.<ref>PMID:12353035</ref>		[[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:[http://omim.org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.<ref>PMID:12353035</ref>
Line 39:		Line 39:
	[[Category: Autographa californica nucleopolyhedrovirus]]		[[Category: Autographa californica nucleopolyhedrovirus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Eliezer, D.]]		[[Category: Eliezer, D]]
	[[Category: Lu, M.]]		[[Category: Lu, M]]
	[[Category: Min, T.]]		[[Category: Min, T]]
	[[Category: Wu, H.]]		[[Category: Wu, H]]
	[[Category: Apoptosis-hydrolase complex]]		[[Category: Apoptosis-hydrolase complex]]
	[[Category: Apoptosis/hydrolase]]		[[Category: Apoptosis/hydrolase]]

OCA at 08:44, 30 September 2014

2014-09-30T08:44:23Z

← Older revision		Revision as of 08:44, 30 September 2014
Line 1:		Line 1:
	~~{{STRUCTURE_2fun~~\| ~~PDB~~=2fun \| ~~SCENE~~= }}		==alternative p35-caspase-8 complex==
	===~~alternative p35~~-~~caspase~~-8 complex===		<StructureSection load='2fun' size='340' side='right' caption='[[2fun]], [[Resolution\|resolution]] 3.00Å' scene=''>
	~~{{ABSTRACT_PUBMED_16492559}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2fun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUN FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1i4e\|1i4e]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 Autographa californica nucleopolyhedrovirus])</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=2fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fun RCSB], [http://www.ebi.ac.uk/pdbsum/2fun PDBsum]</span></td></tr>
			<table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:[http://omim.org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.<ref>PMID:12353035</ref>
			== Function ==
			[[http://www.uniprot.org/uniprot/VP35_NPVAC VP35_NPVAC]] Blocks the insect or worm host cells apoptotic response initiated by the viral infection. Confers protection from cell death in mammalian cells. Acts by blocking the activity of members of the caspase family of proteases. Required for late and very late gene expression. [[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-\|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.<ref>PMID:12010809</ref> <ref>PMID:9006941</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/fu/2fun_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 ==
			Wide-spectrum caspase inhibition by the baculoviral p35 protein was previously shown to be a consequence of covalent inhibition in which a thioester bond is stably formed between the cleavage residue Asp87 of p35 and the active site Cys360' of caspase-8. Here we show that the N-terminal fragment of cleaved p35 (p35-N) is a circular peptide when dissociated from the caspase. Biochemical and crystallographic data suggest that p35-N circularization results from the trapping of a native chemical ligation intermediate in the p35/caspase complex, in which the N-terminal Cys2 of p35 attacks the Asp87-Cys360' thioester to form an equilibrium between Asp87-Cys2 and Asp87-Cys360'. This provides a crucial covalent interaction for keeping the N terminus of p35 bound in the caspase active site, which explains the absolute requirement of Cys2 for caspase inhibition. Participation of native chemical ligation in caspase inhibition by p35 illustrates an unusual mechanism of protease inhibition.

	~~==Disease==~~		Native chemical ligation in covalent caspase inhibition by p35.,Lu M, Min T, Eliezer D, Wu H Chem Biol. 2006 Feb;13(2):117-22. PMID:16492559<ref>PMID:16492559</ref>
	~~[[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects~~ in ~~CASP8 are the cause of~~ caspase~~-8 deficiency (CASP8D) [MIM:[http://omim~~.~~org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy~~, ~~splenomegaly~~, ~~and defective CD95-induced apoptosis of peripheral blood lymphocytes~~ (~~PBLs~~)~~. It leads to defects in activation of T-lymphocytes, B~~-~~lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization~~.<ref>PMID:~~12353035~~</ref>

	~~==Function==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[http:~~//www.uniprot.org/uniprot/VP35_NPVAC VP35_NPVAC]] Blocks the insect or worm host cells apoptotic response initiated by the viral infection. Confers protection from cell death in mammalian cells. Acts by blocking the activity of members of the caspase family of proteases. Required for late and very late gene expression. [[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the ~~GZMB apoptotic pathways. Cleaves ADPRT~~. ~~Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-\|-AMC~~. ~~Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity~~ of ~~the complex~~.<~~ref~~>~~PMID:12010809~~</~~ref><ref~~>~~PMID:9006941</ref>~~		</div>

	~~==About this Structure==~~
	[[2fun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA].

	==See Also==		==See Also==
	*[[Caspase\|Caspase]]		*[[Caspase\|Caspase]]
	*[[User:Christopher French\|User:Christopher French]]		*[[User:Christopher French\|User:Christopher French]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:016492559</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Autographa californica nucleopolyhedrovirus]]		[[Category: Autographa californica nucleopolyhedrovirus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 11:10, 24 March 2013

2013-03-24T11:10:24Z

← Older revision		Revision as of 11:10, 24 March 2013
Line 2:		Line 2:
	===alternative p35-caspase-8 complex===		===alternative p35-caspase-8 complex===
	{{ABSTRACT_PUBMED_16492559}}		{{ABSTRACT_PUBMED_16492559}}

			==Disease==
			[[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Defects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:[http://omim.org/entry/607271 607271]]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.<ref>PMID:12353035</ref>

			==Function==
			[[http://www.uniprot.org/uniprot/VP35_NPVAC VP35_NPVAC]] Blocks the insect or worm host cells apoptotic response initiated by the viral infection. Confers protection from cell death in mammalian cells. Acts by blocking the activity of members of the caspase family of proteases. Required for late and very late gene expression. [[http://www.uniprot.org/uniprot/CASP8_HUMAN CASP8_HUMAN]] Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-\|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.<ref>PMID:12010809</ref><ref>PMID:9006941</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 17:

	==Reference==		==Reference==
	<ref group="xtra">PMID:016492559</ref><references group="xtra"/>		<ref group="xtra">PMID:016492559</ref><references group="xtra"/><references/>
	[[Category: Autographa californica nucleopolyhedrovirus]]		[[Category: Autographa californica nucleopolyhedrovirus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 09:53, 11 March 2013

2013-03-11T09:53:53Z

← Older revision		Revision as of 09:53, 11 March 2013
Line 1:		Line 1:
	~~[[Image:2fun.png\|left\|200px]]~~

	{{STRUCTURE_2fun\| PDB=2fun \| SCENE= }}		{{STRUCTURE_2fun\| PDB=2fun \| SCENE= }}

	===alternative p35-caspase-8 complex===		===alternative p35-caspase-8 complex===

	{{ABSTRACT_PUBMED_16492559}}		{{ABSTRACT_PUBMED_16492559}}

OCA at 05:36, 20 October 2012

2012-10-20T05:36:39Z

← Older revision		Revision as of 05:36, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[2fun]] is a 4 chain structure ~~of [[Caspase]]~~ with sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA].		[[2fun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Autographa_californica_nucleopolyhedrovirus Autographa californica nucleopolyhedrovirus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUN OCA].

	==See Also==		==See Also==
	*[[Caspase\|Caspase]]		*[[Caspase\|Caspase]]
			*[[User:Christopher French\|User:Christopher French]]

	==Reference==		==Reference==