1e41 - Revision history

OCA at 05:29, 15 May 2024

2024-05-15T05:29:52Z

←Older revision		Revision as of 05:29, 15 May 2024
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e41 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=1e41 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	FADD (also known as MORT-1) is an essential adapter protein that couples the transmembrane receptors Fas (CD95) and tumor necrosis factor receptor-1 (TNF-R1) to intracellular cysteine proteases known as caspases, which propagate and execute the programmed cell death-inducing signal triggered by Fas ligand (FasL, CD95L) and TNF. FADD contains 208 amino acid residues, and comprises two functionally and structurally distinct domains: an N-terminal death effector domain (DED) that promotes activation of the downstream proteolytic cascade through binding of the DED domains of procaspase-8; and a C-terminal death domain (DD). FADD-DD provides the site of FADD recruitment to death receptor complexes at the plasma membrane by, for example, interaction with the Fas receptor cytoplasmic death domain (Fas-DD), or binding of the TNF-R1 adapter molecule TRADD. We have determined the three-dimensional solution structure and characterised the internal polypeptide dynamics of human FADD-DD using heteronuclear NMR spectroscopy of (15)N and (13)C,(15)N-labelled samples. The structure comprises six alpha-helices joined by short loops and displays overall similarity to the death domain of the Fas receptor. The analysis of the dynamic properties reveals no evidence of contiguous stretches of polypeptide chain with increased internal motion, except at the extreme chain termini. A pattern of increased rates of amide proton solvent exchange in the alpha3 helix correlates with a higher degree of solvent exposure for this secondary structure element. The properties of the FADD-DD structure are discussed with respect to previously reported mutagenesis data and emerging models for FasL-induced FADD recruitment to Fas and caspase-8 activation.
		+
		+	The three-dimensional solution structure and dynamic properties of the human FADD death domain.,Berglund H, Olerenshaw D, Sankar A, Federwisch M, McDonald NQ, Driscoll PC J Mol Biol. 2000 Sep 8;302(1):171-88. PMID:10964568<ref>PMID:10964568</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1e41" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:58, 20 March 2024

2024-03-20T09:58:16Z

←Older revision		Revision as of 09:58, 20 March 2024
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	==Death domain from human FADD/MORT1==		==Death domain from human FADD/MORT1==
-	<StructureSection load='1e41' size='340' side='right'caption='[[1e41~~]], [[NMR_Ensembles_of_Models \| 25 NMR models~~]]' scene=''>	+	<StructureSection load='1e41' size='340' side='right'caption='[[1e41]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E41 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E41 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;'>[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</div~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [https://pdbe.org/1e41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [https://www.ebi.ac.uk/pdbsum/1e41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e41 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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [https://pdbe.org/1e41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [https://www.ebi.ac.uk/pdbsum/1e41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e41 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/FADD_HUMAN FADD_HUMAN] Defects in FADD are the cause of infections recurrent associated with encephalopathy hepatic dysfunction and cardiovascular malformations (IEHDCM) [MIM:[https://omim.org/entry/613759 613759]. A condition with biological features of autoimmune lymphoproliferative syndrome such as high-circulating CD4(-)CD8(-)TCR-alpha-beta(+) T-cell counts, and elevated IL10 and FASL levels. Affected individuals suffer from recurrent, stereotypical episodes of fever, encephalopathy, and mild liver dysfunction sometimes accompanied by generalized seizures. The episodes can be triggered by varicella zoster virus (VZV), measles mumps rubella (MMR) attenuated vaccine, parainfluenza virus, and Epstein-Barr virus (EBV).<ref>PMID:21109225</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/FADD_HUMAN FADD_HUMAN] Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling.<ref>PMID:21109225</ref> <ref>PMID:16762833</ref> <ref>PMID:19118384</ref> <ref>PMID:20935634</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e41 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=1e41 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	FADD (also known as MORT-1) is an essential adapter protein that couples the transmembrane receptors Fas (CD95) and tumor necrosis factor receptor-1 (TNF-R1) to intracellular cysteine proteases known as caspases, which propagate and execute the programmed cell death-inducing signal triggered by Fas ligand (FasL, CD95L) and TNF. FADD contains 208 amino acid residues, and comprises two functionally and structurally distinct domains: an N-terminal death effector domain (DED) that promotes activation of the downstream proteolytic cascade through binding of the DED domains of procaspase-8; and a C-terminal death domain (DD). FADD-DD provides the site of FADD recruitment to death receptor complexes at the plasma membrane by, for example, interaction with the Fas receptor cytoplasmic death domain (Fas-DD), or binding of the TNF-R1 adapter molecule TRADD. We have determined the three-dimensional solution structure and characterised the internal polypeptide dynamics of human FADD-DD using heteronuclear NMR spectroscopy of (15)N and (13)C,(15)N-labelled samples. The structure comprises six alpha-helices joined by short loops and displays overall similarity to the death domain of the Fas receptor. The analysis of the dynamic properties reveals no evidence of contiguous stretches of polypeptide chain with increased internal motion, except at the extreme chain termini. A pattern of increased rates of amide proton solvent exchange in the alpha3 helix correlates with a higher degree of solvent exposure for this secondary structure element. The properties of the FADD-DD structure are discussed with respect to previously reported mutagenesis data and emerging models for FasL-induced FADD recruitment to Fas and caspase-8 activation.
-
-	The three-dimensional solution structure and dynamic properties of the human FADD death domain.,Berglund H, Olerenshaw D, Sankar A, Federwisch M, McDonald NQ, Driscoll PC J Mol Biol. 2000 Sep 8;302(1):171-88. PMID:10964568<ref>PMID:10964568</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1e41" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Berglund, H]]	+	[[Category: Berglund H]]
-	[[Category: Driscoll~~, P C~~]]	+	[[Category: Driscoll PC]]
-	[[Category: McDonald~~, N Q~~]]	+	[[Category: McDonald NQ]]
-	[[Category: Olerenshaw, D]]	+	[[Category: Olerenshaw D]]
-	~~[[Category: Adapter molecule]]~~	+
-	~~[[Category: Apoptosis]]~~	+
-	~~[[Category: Death domain]]~~	+
-	~~[[Category: Fas receptor death inducing signalling complex~~]]	+

OCA at 09:34, 21 July 2021

2021-07-21T09:34:01Z

←Older revision		Revision as of 09:34, 21 July 2021
Line 3:		Line 3:
	<StructureSection load='1e41' size='340' side='right'caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>		<StructureSection load='1e41' size='340' side='right'caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1E41 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E41 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</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;'>[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [~~http~~://pdbe.org/1e41 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1e41 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1e41 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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [https://pdbe.org/1e41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [https://www.ebi.ac.uk/pdbsum/1e41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e41 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 14:47, 16 October 2019

2019-10-16T14:47:15Z

←Older revision		Revision as of 14:47, 16 October 2019
Line 1:		Line 1:

	==Death domain from human FADD/MORT1==		==Death domain from human FADD/MORT1==
-	<StructureSection load='1e41' size='340' side='right' caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>	+	<StructureSection load='1e41' size='340' side='right'caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>
Line 31:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Berglund, H]]		[[Category: Berglund, H]]
	[[Category: Driscoll, P C]]		[[Category: Driscoll, P C]]

OCA at 08:06, 13 December 2017

2017-12-13T08:06:13Z

←Older revision		Revision as of 08:06, 13 December 2017
Line 1:		Line 1:
-	==~~DEATH DOMAIN FROM HUMAN~~ FADD/MORT1==	+
		+	==Death domain from human FADD/MORT1==
	<StructureSection load='1e41' size='340' side='right' caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>		<StructureSection load='1e41' size='340' side='right' caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [http://pdbe.org/1e41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [http://www.ebi.ac.uk/pdbsum/1e41 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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [http://pdbe.org/1e41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [http://www.ebi.ac.uk/pdbsum/1e41 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e41 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 10:		Line 11:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/1e41_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/1e41_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 32:		Line 33:
	[[Category: Berglund, H]]		[[Category: Berglund, H]]
	[[Category: Driscoll, P C]]		[[Category: Driscoll, P C]]
-	[[Category: ~~Mcdonald~~, N Q]]	+	[[Category: McDonald, N Q]]
	[[Category: Olerenshaw, D]]		[[Category: Olerenshaw, D]]
	[[Category: Adapter molecule]]		[[Category: Adapter molecule]]

OCA at 17:50, 7 February 2016

2016-02-07T17:50:26Z

←Older revision		Revision as of 17:50, 7 February 2016
Line 14:		Line 14:
	<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=1e41 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 03:47, 10 September 2015

2015-09-10T03:47:06Z

←Older revision		Revision as of 03:47, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1e41' size='340' side='right' caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>		<StructureSection load='1e41' size='340' side='right' caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [http://www.ebi.ac.uk/pdbsum/1e41 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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [http://pdbe.org/1e41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [http://www.ebi.ac.uk/pdbsum/1e41 PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 24:		Line 24:
	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 1e41" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Berglund, H]]		[[Category: Berglund, H]]
	[[Category: Driscoll, P C]]		[[Category: Driscoll, P C]]

OCA at 00:47, 23 December 2014

2014-12-23T00:47:44Z

←Older revision		Revision as of 00:47, 23 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [http://www.ebi.ac.uk/pdbsum/1e41 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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [http://www.ebi.ac.uk/pdbsum/1e41 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Berglund, H.]]	+	[[Category: Berglund, H]]
-	[[Category: Driscoll, P C.]]	+	[[Category: Driscoll, P C]]
-	[[Category: Mcdonald, N Q.]]	+	[[Category: Mcdonald, N Q]]
-	[[Category: Olerenshaw, D.]]	+	[[Category: Olerenshaw, D]]
	[[Category: Adapter molecule]]		[[Category: Adapter molecule]]
	[[Category: Apoptosis]]		[[Category: Apoptosis]]
	[[Category: Death domain]]		[[Category: Death domain]]
	[[Category: Fas receptor death inducing signalling complex]]		[[Category: Fas receptor death inducing signalling complex]]

OCA at 17:39, 29 September 2014

2014-09-29T17:39:27Z

←Older revision		Revision as of 17:39, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1e41~~\| ~~PDB~~=1e41 \| ~~SCENE~~= }}	+	==DEATH DOMAIN FROM HUMAN FADD/MORT1==
-	===~~DEATH DOMAIN FROM HUMAN FADD~~/~~MORT1~~===	+	<StructureSection load='1e41' size='340' side='right' caption='[[1e41]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_10964568}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1e41]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E41 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a1w\|1a1w]], [[1a1z\|1a1z]], [[1e3y\|1e3y]]</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=1e41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e41 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e41 RCSB], [http://www.ebi.ac.uk/pdbsum/1e41 PDBsum]</span></td></tr>
		+	<table>
		+	== 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/e4/1e41_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 ==
		+	FADD (also known as MORT-1) is an essential adapter protein that couples the transmembrane receptors Fas (CD95) and tumor necrosis factor receptor-1 (TNF-R1) to intracellular cysteine proteases known as caspases, which propagate and execute the programmed cell death-inducing signal triggered by Fas ligand (FasL, CD95L) and TNF. FADD contains 208 amino acid residues, and comprises two functionally and structurally distinct domains: an N-terminal death effector domain (DED) that promotes activation of the downstream proteolytic cascade through binding of the DED domains of procaspase-8; and a C-terminal death domain (DD). FADD-DD provides the site of FADD recruitment to death receptor complexes at the plasma membrane by, for example, interaction with the Fas receptor cytoplasmic death domain (Fas-DD), or binding of the TNF-R1 adapter molecule TRADD. We have determined the three-dimensional solution structure and characterised the internal polypeptide dynamics of human FADD-DD using heteronuclear NMR spectroscopy of (15)N and (13)C,(15)N-labelled samples. The structure comprises six alpha-helices joined by short loops and displays overall similarity to the death domain of the Fas receptor. The analysis of the dynamic properties reveals no evidence of contiguous stretches of polypeptide chain with increased internal motion, except at the extreme chain termini. A pattern of increased rates of amide proton solvent exchange in the alpha3 helix correlates with a higher degree of solvent exposure for this secondary structure element. The properties of the FADD-DD structure are discussed with respect to previously reported mutagenesis data and emerging models for FasL-induced FADD recruitment to Fas and caspase-8 activation.

-	~~==About this Structure==~~	+	The three-dimensional solution structure and dynamic properties of the human FADD death domain.,Berglund H, Olerenshaw D, Sankar A, Federwisch M, McDonald NQ, Driscoll PC J Mol Biol. 2000 Sep 8;302(1):171-88. PMID:10964568<ref>PMID:10964568</ref>
-	~~[[1e41]] is a 1 chain~~ structure ~~with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full experimental information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1E41 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:010964568</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Berglund, H.]]		[[Category: Berglund, H.]]

OCA at 22:39, 24 March 2013

2013-03-24T22:39:13Z

←Older revision		Revision as of 22:39, 24 March 2013
Line 1:		Line 1:
-	[[Image:1e41.png\|left\|200px]]
-
	{{STRUCTURE_1e41\| PDB=1e41 \| SCENE= }}		{{STRUCTURE_1e41\| PDB=1e41 \| SCENE= }}
-
	===DEATH DOMAIN FROM HUMAN FADD/MORT1===		===DEATH DOMAIN FROM HUMAN FADD/MORT1===
-
	{{ABSTRACT_PUBMED_10964568}}		{{ABSTRACT_PUBMED_10964568}}

Line 11:		Line 7:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010964568</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010964568</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Berglund, H.]]		[[Category: Berglund, H.]]