1jiq - Revision history

OCA at 07:15, 25 October 2023

2023-10-25T07:15:24Z

← Older revision		Revision as of 07:15, 25 October 2023
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	<StructureSection load='1jiq' size='340' side='right'caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1jiq' size='340' side='right'caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>
	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~=~~'plainlinks'~~>~~[https://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose~~-~~6-phosphate isomerase]~~, ~~with EC number~~ [~~https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.~~1.9 ~~5.3.1.9] </span>~~</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [https://pdbe.org/1jiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [https://www.ebi.ac.uk/pdbsum/1jiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jiq 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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [https://pdbe.org/1jiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [https://www.ebi.ac.uk/pdbsum/1jiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jiq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[https://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.		[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[https://omim.org/entry/613470 613470]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref>		[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Glucose-6-phosphate isomerase]]~~		[[Category: Homo sapiens]]
	~~[[Category: Human~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Akiyama, H]]		[[Category: Akiyama H]]
	[[Category: Funasaka, T]]		[[Category: Funasaka T]]
	[[Category: Haga, A]]		[[Category: Haga A]]
	[[Category: Nagase, H]]		[[Category: Nagase H]]
	[[Category: Nakamura~~, K T~~]]		[[Category: Nakamura KT]]
	[[Category: Raz, A]]		[[Category: Raz A]]
	[[Category: Tanaka, N]]		[[Category: Tanaka N]]
	[[Category: Uemura, H]]		[[Category: Uemura H]]
	~~[[Category: Autocrine motility factor]]~~
	~~[[Category: Cytokine]]~~
	~~[[Category: Isomerase~~]]

OCA at 06:41, 11 August 2021

2021-08-11T06:41:16Z

← Older revision		Revision as of 06:41, 11 August 2021
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	<StructureSection load='1jiq' size='340' side='right'caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1jiq' size='340' side='right'caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [~~http~~://pdbe.org/1jiq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1jiq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1jiq 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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [https://pdbe.org/1jiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [https://www.ebi.ac.uk/pdbsum/1jiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jiq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[~~http~~://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.		[[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[https://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref>		[[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Phosphoglucoisomerase\|Phosphoglucoisomerase]]		*[[Phosphoglucose isomerase 3D structures\|Phosphoglucose isomerase 3D structures]]
	*[[Phosphoglucose isomerase\|Phosphoglucose isomerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:24, 6 November 2019

2019-11-06T09:24:20Z

← Older revision		Revision as of 09:24, 6 November 2019
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	==Crystal Structure of Human Autocrine Motility Factor==		==Crystal Structure of Human Autocrine Motility Factor==
	<StructureSection load='1jiq' size='340' side='right' caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1jiq' size='340' side='right'caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>
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	==See Also==		==See Also==
	*[[Phosphoglucoisomerase\|Phosphoglucoisomerase]]		*[[Phosphoglucoisomerase\|Phosphoglucoisomerase]]
			*[[Phosphoglucose isomerase\|Phosphoglucose isomerase]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Glucose-6-phosphate isomerase]]		[[Category: Glucose-6-phosphate isomerase]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Akiyama, H]]		[[Category: Akiyama, H]]
	[[Category: Funasaka, T]]		[[Category: Funasaka, T]]

OCA at 08:59, 17 January 2018

2018-01-17T08:59:45Z

← Older revision		Revision as of 08:59, 17 January 2018
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	==Crystal Structure of Human Autocrine Motility Factor==		==Crystal Structure of Human Autocrine Motility Factor==
	<StructureSection load='1jiq' size='340' side='right' caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1jiq' size='340' side='right' caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>
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	<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [http://pdbe.org/1jiq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [http://www.ebi.ac.uk/pdbsum/1jiq 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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [http://pdbe.org/1jiq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [http://www.ebi.ac.uk/pdbsum/1jiq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jiq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/1jiq_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/1jiq_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>
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	==See Also==		==See Also==
	*[[Phosphoglucoisomerase\|Phosphoglucoisomerase]]		*[[Phosphoglucoisomerase\|Phosphoglucoisomerase]]
	*[[Phosphoglucose isomerase\|Phosphoglucose isomerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:14, 9 February 2016

2016-02-09T15:14:07Z

← Older revision		Revision as of 15:14, 9 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jiq ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 23:28, 10 September 2015

2015-09-10T23:28:27Z

← Older revision		Revision as of 23:28, 10 September 2015
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	<StructureSection load='1jiq' size='340' side='right' caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1jiq' size='340' side='right' caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [http://www.ebi.ac.uk/pdbsum/1jiq 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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [http://pdbe.org/1jiq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [http://www.ebi.ac.uk/pdbsum/1jiq PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 1jiq" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	</StructureSection>		</StructureSection>
	[[Category: Glucose-6-phosphate isomerase]]		[[Category: Glucose-6-phosphate isomerase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Akiyama, H]]		[[Category: Akiyama, H]]
	[[Category: Funasaka, T]]		[[Category: Funasaka, T]]

OCA at 12:00, 2 January 2015

2015-01-02T12:00:16Z

← Older revision		Revision as of 12:00, 2 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [http://www.ebi.ac.uk/pdbsum/1jiq 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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [http://www.ebi.ac.uk/pdbsum/1jiq PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[http://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.		[[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[http://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.
Line 38:		Line 38:
	[[Category: Glucose-6-phosphate isomerase]]		[[Category: Glucose-6-phosphate isomerase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Akiyama, H.]]		[[Category: Akiyama, H]]
	[[Category: Funasaka, T.]]		[[Category: Funasaka, T]]
	[[Category: Haga, A.]]		[[Category: Haga, A]]
	[[Category: Nagase, H.]]		[[Category: Nagase, H]]
	[[Category: Nakamura, K T.]]		[[Category: Nakamura, K T]]
	[[Category: Raz, A.]]		[[Category: Raz, A]]
	[[Category: Tanaka, N.]]		[[Category: Tanaka, N]]
	[[Category: Uemura, H.]]		[[Category: Uemura, H]]
	[[Category: Autocrine motility factor]]		[[Category: Autocrine motility factor]]
	[[Category: Cytokine]]		[[Category: Cytokine]]
	[[Category: Isomerase]]		[[Category: Isomerase]]

OCA at 14:38, 29 September 2014

2014-09-29T14:38:11Z

← Older revision		Revision as of 14:38, 29 September 2014
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	~~{{STRUCTURE_1jiq\| PDB=1jiq \| SCENE= }}~~		==Crystal Structure of Human Autocrine Motility Factor==
	===Crystal Structure of Human Autocrine Motility Factor===		<StructureSection load='1jiq' size='340' side='right' caption='[[1jiq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	~~{{ABSTRACT_PUBMED_12054796}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[1jiq]] is a 4 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=1JIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JIQ FirstGlance]. <br>
	==Disease==		</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></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=1jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jiq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jiq RCSB], [http://www.ebi.ac.uk/pdbsum/1jiq PDBsum]</span></td></tr>
			<table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[http://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.		[[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[http://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.
			== Function ==
			[[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/1jiq_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 ==
			Autocrine motility factor (AMF), a tumor-secreted cytokine, stimulates cell migration in vitro and metastasis in vivo. AMF is genetically identical with the extracellular cytokines neuroleukin (NLK) and maturation factor (MF) and, interestingly, the intracellular enzyme phosphohexose isomerase (PHI). The crystal structures of the inhibitor-free open form and the inhibitor (erythrose 4-phosphate, E4P, a strong inhibitor of AMF's cytokine activity)-bound closed form of human AMF have been determined at 1.9 A and 2.4 A resolution, respectively. Upon E4P binding, local conformation changes (open to closed) occur around the inhibitor-binding site. The E4P-bound structure shows that the location of the inhibitor (of cytokine activity) binding site of human AMF is very similar to those of the inhibitor (of enzymatic activity) binding sites of PHIs. The present study shows clearly that there is structural overlap of the regions responsible for the enzymatic and cytokine functions of AMF and PHI and suggests two scenarios for the inhibition mechanism of cytokine activity of AMF by the carbohydrate phosphate group. One likely scenario is that the compound could compete for AMF binding with the carbohydrate moiety of the AMF receptor (AMFR), which is a glycosylated seven-transmembrane helix protein. The other scenario is that the local conformation changes upon inhibitor binding may affect the AMF-AMFR interactions. To examine roles of the residues in the inhibitor-binding site, two mutant AMFs were prepared. Replacements of His389, which is hydrogen-bonded to the hydroxyl group of E4P by Phe, and Thr215, which is hydrogen-bonded to the phosphate group of E4P by Asp, result in mutant AMFs that are impaired in cytokine activity. These results suggest a role for these amino acids in recognition of a carbohydrate moiety of the AMFR. Since the E4P is one of the smallest compounds having AMF inhibitor activity, knowledge of the present crystal structure would provide an insight into the lead compound design of more effective AMF inhibitors.

	~~==Function==~~		Inhibition mechanism of cytokine activity of human autocrine motility factor examined by crystal structure analyses and site-directed mutagenesis studies.,Tanaka N, Haga A, Uemura H, Akiyama H, Funasaka T, Nagase H, Raz A, Nakamura KT J Mol Biol. 2002 May 10;318(4):985-97. PMID:12054796<ref>PMID:12054796</ref>
	~~[[http://www~~.~~uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Besides it's role as a glycolytic enzyme~~, ~~mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility~~. ~~GPI is also a neurotrophic factor~~ (~~Neuroleukin~~) ~~for spinal and sensory neurons~~.~~<ref>~~PMID:~~11004567</ref><ref>PMID:11437381</ref>~~<ref>PMID:~~12163179~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[1jiq]] is~~ a ~~4 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=1JIQ OCA].~~		</div>

	==See Also==		==See Also==
	*[[Phosphoglucoisomerase\|Phosphoglucoisomerase]]		*[[Phosphoglucoisomerase\|Phosphoglucoisomerase]]
			*[[Phosphoglucose isomerase\|Phosphoglucose isomerase]]
	==~~Reference~~==		== References ==
	~~<ref group="xtra">PMID:012054796</ref>~~<references ~~group="xtra"~~/><~~references~~/>		<references/>
			__TOC__
			</StructureSection>
	[[Category: Glucose-6-phosphate isomerase]]		[[Category: Glucose-6-phosphate isomerase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 11:16, 24 March 2013

2013-03-24T11:16:24Z

← Older revision		Revision as of 11:16, 24 March 2013
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	===Crystal Structure of Human Autocrine Motility Factor===		===Crystal Structure of Human Autocrine Motility Factor===
	{{ABSTRACT_PUBMED_12054796}}		{{ABSTRACT_PUBMED_12054796}}

			==Disease==
			[[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[http://omim.org/entry/613470 613470]]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.

			==Function==
			[[http://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN]] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref><ref>PMID:11437381</ref><ref>PMID:12163179</ref>

	==About this Structure==		==About this Structure==
Line 10:		Line 16:

	==Reference==		==Reference==
	<ref group="xtra">PMID:012054796</ref><references group="xtra"/>		<ref group="xtra">PMID:012054796</ref><references group="xtra"/><references/>
	[[Category: Glucose-6-phosphate isomerase]]		[[Category: Glucose-6-phosphate isomerase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 09:56, 11 March 2013

2013-03-11T09:56:20Z

← Older revision		Revision as of 09:56, 11 March 2013
Line 1:		Line 1:
	~~[[Image:1jiq.png\|left\|200px]]~~

	{{STRUCTURE_1jiq\| PDB=1jiq \| SCENE= }}		{{STRUCTURE_1jiq\| PDB=1jiq \| SCENE= }}

	===Crystal Structure of Human Autocrine Motility Factor===		===Crystal Structure of Human Autocrine Motility Factor===

	{{ABSTRACT_PUBMED_12054796}}		{{ABSTRACT_PUBMED_12054796}}