1fyx - Revision history

OCA at 11:18, 27 March 2024

OCA — Wed, 27 Mar 2024 11:18:09 GMT

←Older revision		Revision as of 11:18, 27 March 2024
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	<StructureSection load='1fyx' size='340' side='right'caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1fyx' size='340' side='right'caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=CAS:S~~-~~(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.8Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1fyv\|1fyv]], [[1fyw\|1fyw]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [https://pdbe.org/1fyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [https://www.ebi.ac.uk/pdbsum/1fyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fyx 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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [https://pdbe.org/1fyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [https://www.ebi.ac.uk/pdbsum/1fyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fyx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TLR2_HUMAN TLR2_HUMAN]] Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6.	+	[https://www.uniprot.org/uniprot/TLR2_HUMAN TLR2_HUMAN] Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fyx 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=1fyx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Toll-like receptors (TLRs) and the interleukin-1 receptor superfamily (IL-1Rs) are integral to both innate and adaptive immunity for host defence. These receptors share a conserved cytoplasmic domain, known as the TIR domain. A single-point mutation in the TIR domain of murine TLR4 (Pro712His, the Lps(d) mutation) abolishes the host immune response to lipopolysaccharide (LPS), and mutation of the equivalent residue in TLR2, Pro681His, disrupts signal transduction in response to stimulation by yeast and gram-positive bacteria. Here we report the crystal structures of the TIR domains of human TLR1 and TLR2 and of the Pro681His mutant of TLR2. The structures have a large conserved surface patch that also contains the site of the Lps(d) mutation. Mutagenesis and functional studies confirm that residues in this surface patch are crucial for receptor signalling. The Lps(d) mutation does not disturb the structure of the TIR domain itself. Instead, structural and functional studies indicate that the conserved surface patch may mediate interactions with the down-stream MyD88 adapter molecule, and that the Lps(d) mutation may abolish receptor signalling by disrupting this recruitment.
-
-	Structural basis for signal transduction by the Toll/interleukin-1 receptor domains.,Xu Y, Tao X, Shen B, Horng T, Medzhitov R, Manley JL, Tong L Nature. 2000 Nov 2;408(6808):111-5. PMID:11081518<ref>PMID:11081518</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1fyx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Toll-like Receptor 3D structures\|Toll-like Receptor 3D structures]]		*[[Toll-like Receptor 3D structures\|Toll-like Receptor 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Horng, T]]	+	[[Category: Horng T]]
-	[[Category: Manley~~, J L~~]]	+	[[Category: Manley JL]]
-	[[Category: Medzhitov, R]]	+	[[Category: Medzhitov R]]
-	[[Category: Shen, B]]	+	[[Category: Shen B]]
-	[[Category: Tao, X]]	+	[[Category: Tao X]]
-	[[Category: Tong, L]]	+	[[Category: Tong L]]
-	[[Category: Xu, Y]]	+	[[Category: Xu Y]]
-	~~[[Category: Beta-alpha-beta fold]]~~	+
-	~~[[Category: Signaling protein~~]]	+

OCA at 06:35, 11 August 2021

OCA — Wed, 11 Aug 2021 06:35:05 GMT

←Older revision		Revision as of 06:35, 11 August 2021
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	<StructureSection load='1fyx' size='340' side='right'caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1fyx' size='340' side='right'caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1FYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fyv\|1fyv]], [[1fyw\|1fyw]]</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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [~~http~~://pdbe.org/1fyx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1fyx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1fyx 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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [https://pdbe.org/1fyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [https://www.ebi.ac.uk/pdbsum/1fyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fyx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TLR2_HUMAN TLR2_HUMAN]] Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6.	+	[[https://www.uniprot.org/uniprot/TLR2_HUMAN TLR2_HUMAN]] Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Toll-like ~~Receptors~~\|Toll-like ~~Receptors~~]]	+	*[[Toll-like Receptor 3D structures\|Toll-like Receptor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:39, 6 November 2019

OCA — Wed, 06 Nov 2019 09:39:40 GMT

←Older revision		Revision as of 09:39, 6 November 2019
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF P681H MUTANT OF TIR DOMAIN OF HUMAN TLR2==		==CRYSTAL STRUCTURE OF P681H MUTANT OF TIR DOMAIN OF HUMAN TLR2==
-	<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='1fyx' size='340' side='right'caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1fyx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1fyx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Toll-like Receptors\|Toll-like Receptors]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Horng, T]]		[[Category: Horng, T]]
	[[Category: Manley, J L]]		[[Category: Manley, J L]]

OCA at 06:18, 31 January 2018

OCA — Wed, 31 Jan 2018 06:18:52 GMT

←Older revision		Revision as of 06:18, 31 January 2018
Line 3:		Line 3:
	<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fyx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</td></tr>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fyx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/1fyx_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 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1fyx" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1fyx" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Toll-like Receptors\|Toll-like Receptors]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Horng, T]]		[[Category: Horng, T]]
	[[Category: Manley, J L]]		[[Category: Manley, J L]]

OCA at 10:53, 13 September 2017

OCA — Wed, 13 Sep 2017 10:53:55 GMT

←Older revision		Revision as of 10:53, 13 September 2017
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF P681H MUTANT OF TIR DOMAIN OF HUMAN TLR2==		==CRYSTAL STRUCTURE OF P681H MUTANT OF TIR DOMAIN OF HUMAN TLR2==
	<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fyx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://pdbe.org/1fyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx 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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://pdbe.org/1fyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fyx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<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=1fyx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]
	[[Category: Horng, T]]		[[Category: Horng, T]]
	[[Category: Manley, J L]]		[[Category: Manley, J L]]

OCA at 14:06, 11 September 2015

OCA — Fri, 11 Sep 2015 14:06:01 GMT

←Older revision		Revision as of 14:06, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx 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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://pdbe.org/1fyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1fyx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Horng, T]]		[[Category: Horng, T]]
	[[Category: Manley, J L]]		[[Category: Manley, J L]]

OCA at 17:29, 25 December 2014

OCA — Thu, 25 Dec 2014 17:29:15 GMT

←Older revision		Revision as of 17:29, 25 December 2014
Line 7:		Line 7:
	<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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx 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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TLR2_HUMAN TLR2_HUMAN]] Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:22, 22 December 2014

OCA — Mon, 22 Dec 2014 22:22:16 GMT

←Older revision		Revision as of 22:22, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx 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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx 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 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Horng, T.]]	+	[[Category: Horng, T]]
-	[[Category: Manley, J L.]]	+	[[Category: Manley, J L]]
-	[[Category: Medzhitov, R.]]	+	[[Category: Medzhitov, R]]
-	[[Category: Shen, B.]]	+	[[Category: Shen, B]]
-	[[Category: Tao, X.]]	+	[[Category: Tao, X]]
-	[[Category: Tong, L.]]	+	[[Category: Tong, L]]
-	[[Category: Xu, Y.]]	+	[[Category: Xu, Y]]
	[[Category: Beta-alpha-beta fold]]		[[Category: Beta-alpha-beta fold]]
	[[Category: Signaling protein]]		[[Category: Signaling protein]]

OCA at 12:13, 28 September 2014

OCA — Sun, 28 Sep 2014 12:13:23 GMT

←Older revision		Revision as of 12:13, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1fyx.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF P681H MUTANT OF TIR DOMAIN OF HUMAN TLR2==
		+	<StructureSection load='1fyx' size='340' side='right' caption='[[1fyx]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1fyx]] is a 1 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=1FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FYX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fyv\|1fyv]], [[1fyw\|1fyw]]</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=1fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fyx RCSB], [http://www.ebi.ac.uk/pdbsum/1fyx 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/fy/1fyx_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 ==
		+	Toll-like receptors (TLRs) and the interleukin-1 receptor superfamily (IL-1Rs) are integral to both innate and adaptive immunity for host defence. These receptors share a conserved cytoplasmic domain, known as the TIR domain. A single-point mutation in the TIR domain of murine TLR4 (Pro712His, the Lps(d) mutation) abolishes the host immune response to lipopolysaccharide (LPS), and mutation of the equivalent residue in TLR2, Pro681His, disrupts signal transduction in response to stimulation by yeast and gram-positive bacteria. Here we report the crystal structures of the TIR domains of human TLR1 and TLR2 and of the Pro681His mutant of TLR2. The structures have a large conserved surface patch that also contains the site of the Lps(d) mutation. Mutagenesis and functional studies confirm that residues in this surface patch are crucial for receptor signalling. The Lps(d) mutation does not disturb the structure of the TIR domain itself. Instead, structural and functional studies indicate that the conserved surface patch may mediate interactions with the down-stream MyD88 adapter molecule, and that the Lps(d) mutation may abolish receptor signalling by disrupting this recruitment.

-	~~{{STRUCTURE_1fyx\| PDB=1fyx \| SCENE= }}~~	+	Structural basis for signal transduction by the Toll/interleukin-1 receptor domains.,Xu Y, Tao X, Shen B, Horng T, Medzhitov R, Manley JL, Tong L Nature. 2000 Nov 2;408(6808):111-5. PMID:11081518<ref>PMID:11081518</ref>

-	~~===CRYSTAL STRUCTURE OF P681H MUTANT OF TIR DOMAIN OF HUMAN TLR2===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11081518}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1fyx]] is~~ a ~~1 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=1FYX OCA].~~	+

	==See Also==		==See Also==
	*[[Toll-like Receptors\|Toll-like Receptors]]		*[[Toll-like Receptors\|Toll-like Receptors]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011081518<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Horng, T.]]		[[Category: Horng, T.]]

OCA at 19:27, 20 October 2012

OCA — Sat, 20 Oct 2012 19:27:21 GMT

←Older revision		Revision as of 19:27, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1fyx]] is a 1 chain structure ~~of [[Toll-like Receptors]]~~ 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=1FYX OCA].	+	[[1fyx]] is a 1 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=1FYX OCA].

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