1alg - Revision history

OCA at 11:32, 22 November 2023

2023-11-22T11:32:52Z

← Older revision		Revision as of 11:32, 22 November 2023
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	==SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES==		==SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES==
	<StructureSection load='1alg' size='340' side='right'caption='[[1alg~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>		<StructureSection load='1alg' size='340' side='right'caption='[[1alg]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Synthetic_construct_sequences~~ Synthetic construct ~~sequences~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALG 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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [https://pdbe.org/1alg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [https://www.ebi.ac.uk/pdbsum/1alg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alg 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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [https://pdbe.org/1alg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [https://www.ebi.ac.uk/pdbsum/1alg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN]] Maintains high levels of reduced glutathione in the cytosol.		[https://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN] Maintains high levels of reduced glutathione in the cytosol.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Glutathione-disulfide reductase]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Synthetic construct ~~sequences~~]]		[[Category: Synthetic construct]]
	[[Category: Becker, K]]		[[Category: Becker K]]
	[[Category: Kalbitzer~~, H R~~]]		[[Category: Kalbitzer HR]]
	[[Category: Nordhoff, A]]		[[Category: Nordhoff A]]
	[[Category: Schirmer~~, R H~~]]		[[Category: Schirmer RH]]
	[[Category: Schott~~, M K]]~~		[[Category: Schott MK]]
	~~[[Category: Human glutathione reductase]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Protein-dimerization inhibitor~~]]

OCA at 10:23, 16 February 2022

2022-02-16T10:23:36Z

← Older revision		Revision as of 10:23, 16 February 2022
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	<StructureSection load='1alg' size='340' side='right'caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1alg' size='340' side='right'caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALG 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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [https://pdbe.org/1alg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [https://www.ebi.ac.uk/pdbsum/1alg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alg 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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [https://pdbe.org/1alg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [https://www.ebi.ac.uk/pdbsum/1alg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alg ProSAT]</span></td></tr>
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	[[Category: Glutathione-disulfide reductase]]		[[Category: Glutathione-disulfide reductase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
			[[Category: Synthetic construct sequences]]
	[[Category: Becker, K]]		[[Category: Becker, K]]
	[[Category: Kalbitzer, H R]]		[[Category: Kalbitzer, H R]]

OCA at 10:21, 17 February 2021

2021-02-17T10:21:40Z

← Older revision		Revision as of 10:21, 17 February 2021
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	<StructureSection load='1alg' size='340' side='right'caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1alg' size='340' side='right'caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ALG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALG 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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [~~http~~://pdbe.org/1alg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1alg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1alg 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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [https://pdbe.org/1alg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [https://www.ebi.ac.uk/pdbsum/1alg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1alg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN]] Maintains high levels of reduced glutathione in the cytosol.		[[https://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN]] Maintains high levels of reduced glutathione in the cytosol.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 15:10, 10 May 2019

2019-05-10T15:10:22Z

← Older revision		Revision as of 15:10, 10 May 2019
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES==		==SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES==
	<StructureSection load='1alg' size='340' side='right' caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1alg' size='340' side='right'caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG FirstGlance]. <br>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Glutathione-disulfide reductase]]		[[Category: Glutathione-disulfide reductase]]
			[[Category: Large Structures]]
	[[Category: Becker, K]]		[[Category: Becker, K]]
	[[Category: Kalbitzer, H R]]		[[Category: Kalbitzer, H R]]

OCA at 09:25, 9 August 2017

2017-08-09T09:25:11Z

← Older revision		Revision as of 09:25, 9 August 2017
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES==		==SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES==
	<StructureSection load='1alg' size='340' side='right' caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1alg' size='340' side='right' caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG 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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://pdbe.org/1alg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg 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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://pdbe.org/1alg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1alg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</StructureSection>		</StructureSection>
	[[Category: Glutathione-disulfide reductase]]		[[Category: Glutathione-disulfide reductase]]
	~~[[Category: Synthetic construct sequences]]~~
	[[Category: Becker, K]]		[[Category: Becker, K]]
	[[Category: Kalbitzer, H R]]		[[Category: Kalbitzer, H R]]

OCA at 08:12, 10 September 2015

2015-09-10T08:12:55Z

← Older revision		Revision as of 08:12, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1alg' size='340' side='right' caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1alg' size='340' side='right' caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Synthetic_construct~~ Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG 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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg 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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://pdbe.org/1alg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	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 1alg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Glutathione-disulfide reductase]]		[[Category: Glutathione-disulfide reductase]]
	[[Category: Synthetic construct]]		[[Category: Synthetic construct sequences]]
	[[Category: Becker, K]]		[[Category: Becker, K]]
	[[Category: Kalbitzer, H R]]		[[Category: Kalbitzer, H R]]

OCA at 20:52, 24 December 2014

2014-12-24T20:52:21Z

← Older revision		Revision as of 20:52, 24 December 2014
Line 6:		Line 6:
	<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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg 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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN]] Maintains high levels of reduced glutathione in the cytosol.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:23, 22 December 2014

2014-12-22T10:23:48Z

← Older revision		Revision as of 10:23, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg 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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg PDBsum]</span></td></tr>
	<table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	[[Category: Glutathione-disulfide reductase]]		[[Category: Glutathione-disulfide reductase]]
	[[Category: Synthetic construct]]		[[Category: Synthetic construct]]
	[[Category: Becker, K.]]		[[Category: Becker, K]]
	[[Category: Kalbitzer, H R.]]		[[Category: Kalbitzer, H R]]
	[[Category: Nordhoff, A.]]		[[Category: Nordhoff, A]]
	[[Category: Schirmer, R H.]]		[[Category: Schirmer, R H]]
	[[Category: Schott, M K.]]		[[Category: Schott, M K]]
	[[Category: Human glutathione reductase]]		[[Category: Human glutathione reductase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Protein-dimerization inhibitor]]		[[Category: Protein-dimerization inhibitor]]

OCA at 08:16, 30 July 2014

2014-07-30T08:16:20Z

← Older revision		Revision as of 08:16, 30 July 2014
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	[[~~Image~~:1alg.~~png\|left\|200px~~]]		==SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES==
			<StructureSection load='1alg' size='340' side='right' caption='[[1alg]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[1alg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALG FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </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=1alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1alg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1alg RCSB], [http://www.ebi.ac.uk/pdbsum/1alg PDBsum]</span></td></tr>
			<table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Human glutathione reductase (GR; which catalyzes the reaction NADPH + GSSG + H+ --> 2 GSH + NADP+) is an obligatory FAD-containing homodimer of known geometry. Native human GR, a potential target of antimalarial and cytostatic agents, cannot be dissociated by dilution or by means of subunit-interface mimetics, similarly to well-studied viral dimeric proteins. However, ab initio folding and/or dimerization of human GR can be inhibited by point mutations or by peptides corresponding to subunit-interface areas, for example synthetic peptide P11, which represents the intersubunit-contact helix H11. The structure of this peptide, which might assist inhibitor design, was solved by high-resolution NMR spectroscopy. Residues 440-453, were found to be alpha helical in the isolated peptide. To quantitate the efficacy of inhibitors such as P11, we developed the following unfolding/reactivation assay. The effects of various guanidine hydrochloride (Gdn/HCl) concentrations were studied by analytical ultracentrifugation. It was shown that human GR denatured by greater than 3 M Gdn/HCl is monomeric and free of FAD. Circular-dichroism experiments at 223 nm indicated a half-life of approximately 20 s at 20 degrees C for the unfolding process. To optimize the reactivation yield, four parameters [protein concentration (x) in the range 0.3-10 microg/ml, cofactor supplementation, temperature (y: 0-32 degrees C), and time (0-72 h)] were varied systematically, and a reactivation score z was given to each constellation of parameters. This type of analysis might be useful to optimize refolding and activation yields for other proteins. For human GR, the highest recovery was found not to occur at one of the corners of the x,y plane, but close to its center. Consequently, the optimal assay conditions for folding and dimerization inhibitors are as follows. The enzyme (at 300 microg/ml) is denatured by 5 M guanidine hydrochloride/5 mM dithiothreitol, then reactivated by dilution to 1 microg/ml at pH 6.9 and 20 degrees C. In the absence of inhibitors, this procedure leads to 70% of the control activity within 8 h. Peptides representing the upper subunit interface (for instance residues 436-478) of human GR were found to inhibit refolding with EC50% values in the micromolar range, whereas fragments from other regions of the protein had no influence on this process. For peptide P11, the EC50% value was 20 microM. In conclusion, hGR, enzyme with a tight intersubunit contact area of 21 nm2, appears to be suitable for studying protein folding, dimerization, and prosthetic-group complexation in the absence and presence of compounds that inhibit these processes. There is a shortage, at least for oligomeric enzymes of eukaryotes, of published systematic studies on protein (re)activation.

	~~{{STRUCTURE_1alg\| PDB=1alg \| SCENE= }}~~		Denaturation and reactivation of dimeric human glutathione reductase--an assay for folding inhibitors.,Nordhoff A, Tziatzios C, van den Broek JA, Schott MK, Kalbitzer HR, Becker K, Schubert D, Schirmer RH Eur J Biochem. 1997 Apr 15;245(2):273-82. PMID:9151953<ref>PMID:9151953</ref>

	~~===SOLUTION STRUCTURE OF AN HGR INHIBITOR~~, ~~NMR, 10 STRUCTURES===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_9151953}}~~		==See Also==
			*[[Glutathione Reductase\|Glutathione Reductase]]
	==~~About this Structure~~==		== References ==
	[[~~1alg~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALG OCA].~~		<references/>
			__TOC__
			</StructureSection>
	[[Category: Glutathione-disulfide reductase]]		[[Category: Glutathione-disulfide reductase]]
	[[Category: Synthetic construct]]		[[Category: Synthetic construct]]

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

2012-10-21T12:23:11Z

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

← Older revision	Revision as of 12:23, 21 October 2012
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