1mr8 - Revision history

OCA at 23:43, 27 December 2023

OCA — Wed, 27 Dec 2023 23:43:41 GMT

←Older revision		Revision as of 23:43, 27 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [https://pdbe.org/1mr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [https://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr8 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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [https://pdbe.org/1mr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [https://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/S10A8_HUMAN S10A8_HUMAN]] S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transfering arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread.<ref>PMID:12626582</ref> <ref>PMID:15331440</ref> <ref>PMID:15598812</ref> <ref>PMID:15642721</ref> <ref>PMID:16258195</ref> <ref>PMID:19087201</ref> <ref>PMID:19122197</ref> <ref>PMID:19935772</ref> <ref>PMID:21487906</ref> <ref>PMID:22808130</ref> <ref>PMID:22363402</ref>	+	[https://www.uniprot.org/uniprot/S10A8_HUMAN S10A8_HUMAN] S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transfering arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread.<ref>PMID:12626582</ref> <ref>PMID:15331440</ref> <ref>PMID:15598812</ref> <ref>PMID:15642721</ref> <ref>PMID:16258195</ref> <ref>PMID:19087201</ref> <ref>PMID:19122197</ref> <ref>PMID:19935772</ref> <ref>PMID:21487906</ref> <ref>PMID:22808130</ref> <ref>PMID:22363402</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ishikawa, K]]	+	[[Category: Ishikawa K]]
-	[[Category: Nakagawa, A]]	+	[[Category: Nakagawa A]]
-	[[Category: Nishihira, J]]	+	[[Category: Nishihira J]]
-	[[Category: Tanaka, I]]	+	[[Category: Tanaka I]]
-	~~[[Category: Calcium-binding protein]]~~	+
-	~~[[Category: Mad]]~~	+
-	~~[[Category: Metal transport]]~~	+
-	~~[[Category: Migration inhibitory factor_ related protein 8]]~~	+
-	~~[[Category: S100 protein~~]]	+

OCA at 06:54, 25 August 2021

OCA — Wed, 25 Aug 2021 06:54:47 GMT

←Older revision		Revision as of 06:54, 25 August 2021
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	<StructureSection load='1mr8' size='340' side='right'caption='[[1mr8]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1mr8' size='340' side='right'caption='[[1mr8]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [~~http~~://pdbe.org/1mr8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr8 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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [https://pdbe.org/1mr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [https://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/S10A8_HUMAN S10A8_HUMAN]] S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transfering arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread.<ref>PMID:12626582</ref> <ref>PMID:15331440</ref> <ref>PMID:15598812</ref> <ref>PMID:15642721</ref> <ref>PMID:16258195</ref> <ref>PMID:19087201</ref> <ref>PMID:19122197</ref> <ref>PMID:19935772</ref> <ref>PMID:21487906</ref> <ref>PMID:22808130</ref> <ref>PMID:22363402</ref>	+	[[https://www.uniprot.org/uniprot/S10A8_HUMAN S10A8_HUMAN]] S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transfering arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread.<ref>PMID:12626582</ref> <ref>PMID:15331440</ref> <ref>PMID:15598812</ref> <ref>PMID:15642721</ref> <ref>PMID:16258195</ref> <ref>PMID:19087201</ref> <ref>PMID:19122197</ref> <ref>PMID:19935772</ref> <ref>PMID:21487906</ref> <ref>PMID:22808130</ref> <ref>PMID:22363402</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[S100 ~~protein~~\|S100 ~~protein~~]]	+	*[[S100 proteins 3D structures\|S100 proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:12, 20 November 2019

OCA — Wed, 20 Nov 2019 18:12:49 GMT

←Older revision		Revision as of 18:12, 20 November 2019
Line 1:		Line 1:

	==MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN==		==MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN==
-	<StructureSection load='1mr8' size='340' side='right' caption='[[1mr8]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1mr8' size='340' side='right'caption='[[1mr8]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1mr8" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mr8" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[S100 protein\|S100 protein]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
	[[Category: Ishikawa, K]]		[[Category: Ishikawa, K]]
	[[Category: Nakagawa, A]]		[[Category: Nakagawa, A]]

OCA at 07:41, 31 January 2018

OCA — Wed, 31 Jan 2018 07:41:36 GMT

←Older revision		Revision as of 07:41, 31 January 2018
Line 1:		Line 1:
		+
	==MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN==		==MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN==
	<StructureSection load='1mr8' size='340' side='right' caption='[[1mr8]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1mr8' size='340' side='right' caption='[[1mr8]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://pdbe.org/1mr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr8 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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://pdbe.org/1mr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mr8_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mr8_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 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1mr8" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mr8" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[S100 protein\|S100 protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:07, 7 February 2016

OCA — Sun, 07 Feb 2016 04:07:18 GMT

←Older revision		Revision as of 04:07, 7 February 2016
Line 16:		Line 16:
	<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=1mr8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:38, 9 September 2015

OCA — Wed, 09 Sep 2015 21:38:40 GMT

←Older revision		Revision as of 21:38, 9 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr8 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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://pdbe.org/1mr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr8 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1mr8" style="background-color:#fffaf0;"></div>

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

OCA at 07:43, 24 December 2014

OCA — Wed, 24 Dec 2014 07:43:36 GMT

←Older revision		Revision as of 07:43, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr8 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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr8 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/S10A8_HUMAN S10A8_HUMAN]] S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transfering arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinfammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread.<ref>PMID:12626582</ref> <ref>PMID:15331440</ref> <ref>PMID:15598812</ref> <ref>PMID:15642721</ref> <ref>PMID:16258195</ref> <ref>PMID:19087201</ref> <ref>PMID:19122197</ref> <ref>PMID:19935772</ref> <ref>PMID:21487906</ref> <ref>PMID:22808130</ref> <ref>PMID:22363402</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Ishikawa, K.]]	+	[[Category: Ishikawa, K]]
-	[[Category: Nakagawa, A.]]	+	[[Category: Nakagawa, A]]
-	[[Category: Nishihira, J.]]	+	[[Category: Nishihira, J]]
-	[[Category: Tanaka, I.]]	+	[[Category: Tanaka, I]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Mad]]		[[Category: Mad]]

OCA at 13:37, 28 September 2014

OCA — Sun, 28 Sep 2014 13:37:59 GMT

←Older revision		Revision as of 13:37, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1mr8.~~png\|left~~\|200px]]	+	==MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN==
		+	<StructureSection load='1mr8' size='340' side='right' caption='[[1mr8]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
		+	<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=1mr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr8 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/mr/1mr8_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 ==
		+	The structure of human MRP8 in the calcium-bound form was determined at 1.9 A resolution by X-ray crystallography. The structure was initially solved by MAD phasing of an ytterbium-substituted crystal and was refined against data obtained from a Ca(2+)-bound crystal. The dimeric form of MRP8 was stabilized by hydrophobic interactions between mutually wrapped helices. There were two EF-hand motifs per monomer and each EF-hand bound one Ca(2+) with a different affinity [the affinity of the C-terminal EF-hand (EF-2) for Ca(2+) was stronger than that of the N-terminal EF-hand (EF-1)]. Furthermore, replacement with Yb(3+) occurred in the C-terminal EF-hand only, suggesting a more flexible nature for EF-2 than for EF-1. This, combined with previous observations that the helix in EF-2 (helix III) undergoes a large conformational change upon calcium binding, suggests that the C-terminal EF-hand (EF-2) plays a role as a trigger for Ca(2+)-induced conformational change.

-	~~{{STRUCTURE_1mr8\| PDB=1mr8 \| SCENE= }}~~	+	The structure of human MRP8, a member of the S100 calcium-binding protein family, by MAD phasing at 1.9 A resolution.,Ishikawa K, Nakagawa A, Tanaka I, Suzuki M, Nishihira J Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):559-66. PMID:10771424<ref>PMID:10771424</ref>

-	~~===MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_10771424}}~~	+	==See Also==
-		+	*[[S100 protein\|S100 protein]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1mr8~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:010771424<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ishikawa, K.]]		[[Category: Ishikawa, K.]]

OCA: Protected "1mr8" [edit=sysop:move=sysop]

OCA — Wed, 05 Dec 2012 20:35:40 GMT

Protected "1mr8" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:35, 5 December 2012

OCA at 20:35, 5 December 2012

OCA — Wed, 05 Dec 2012 20:35:37 GMT

←Older revision		Revision as of 20:35, 5 December 2012
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-	{{Seed}}
	[[Image:1mr8.png\|left\|200px]]		[[Image:1mr8.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1mr8", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
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	{{STRUCTURE_1mr8\| PDB=1mr8 \| SCENE= }}		{{STRUCTURE_1mr8\| PDB=1mr8 \| SCENE= }}

	===MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN===		===MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 FROM HUMAN===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_10771424}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 10771424 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_10771424}}		{{ABSTRACT_PUBMED_10771424}}

	==About this Structure==		==About this Structure==
-	~~1MR8~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA].	+	[[1mr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR8 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~10771424~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010771424</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ishikawa, K.]]		[[Category: Ishikawa, K.]]
Line 30:		Line 18:
	[[Category: Tanaka, I.]]		[[Category: Tanaka, I.]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
-	[[Category: Crystal structure]]
	[[Category: Mad]]		[[Category: Mad]]
		+	[[Category: Metal transport]]
	[[Category: Migration inhibitory factor_ related protein 8]]		[[Category: Migration inhibitory factor_ related protein 8]]
	[[Category: S100 protein]]		[[Category: S100 protein]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:06:58 2009''