1auc - Revision history

OCA at 06:33, 7 February 2024

2024-02-07T06:33:18Z

←Older revision		Revision as of 06:33, 7 February 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUC FirstGlance]. <br>
-	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [https://pdbe.org/1auc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [https://www.ebi.ac.uk/pdbsum/1auc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auc ProSAT]</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]] 2.1Å</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [https://pdbe.org/1auc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [https://www.ebi.ac.uk/pdbsum/1auc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>	+	[https://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 18:		Line 19:
	</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=1auc 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=1auc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Thioredoxins are a group of ca. 12 kDa redox proteins that mediate numerous cytosolic processes in all cells. Human thioredoxin can be exported out of the cell where it has additional functions including the ability to stimulate cell growth. A recent crystal structure determination of human thioredoxin revealed an inactive dimeric form of the protein covalently linked through a disulfide bond involving Cys 73 from each monomer [Weichsel et al. (1996) Structure 4, 735-751]. In the present study, apparent dissociation constants (Kapp) for the noncovalently linked dimers were determined at various pHs using a novel assay in which preformed dimers, but not monomers, were rapidly linked through oxidation (with diamide) of the Cys 73 disulfide bond, and the relative amounts of monomer and dimer were detected by gel filtration. The values obtained were pH-dependent, varying between 6.1 and 166 microM for the pH range of 3.8-8.0, and were consistent with the titration of a single ionizable group having a pKa of 6.5. A similar value was obtained using gel filtration at pH 3.8 (Kapp = 164 microM), and the crystal structure of the diamide-oxidized protein was determined to be nearly identical to that obtained in the absence of diamide. Asp 60 lies in the dimer interface and was found to be responsible for the pH dependence for dimer formation, and therefore must have a pKa elevated by approximately 2.5 pH units. Mutation of Asp 60 to asparagine abolished nearly all of the pH dependence for dimer formation. The crystal structure of the D60N mutant revealed a dimer nearly identical to the wild type, but, surprisingly, it had the Asn 60 side chain rotated out of the dimer interface and replaced with two water molecules. The values obtained for Kapp suggest human thioredoxin may dimerize in vivo and possible roles for such dimers are discussed.
-
-	Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant.,Andersen JF, Sanders DA, Gasdaska JR, Weichsel A, Powis G, Montfort WR Biochemistry. 1997 Nov 18;36(46):13979-88. PMID:9369469<ref>PMID:9369469</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1auc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 28:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Anderson~~, J F~~]]	+	[[Category: Anderson JF]]
-	[[Category: Gasdaska, J]]	+	[[Category: Gasdaska J]]
-	[[Category: Montfort~~, W R~~]]	+	[[Category: Montfort WR]]
-	[[Category: Powis, G]]	+	[[Category: Powis G]]
-	[[Category: Sanders~~, D A.R~~]]	+	[[Category: Sanders DAR]]
-	[[Category: Weichsel, A]]	+	[[Category: Weichsel A]]
-	~~[[Category: Dimer]]~~	+
-	~~[[Category: Electron transport]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Thioredoxin~~]]	+

OCA at 16:08, 27 October 2021

2021-10-27T16:08:20Z

←Older revision		Revision as of 16:08, 27 October 2021
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	<StructureSection load='1auc' size='340' side='right'caption='[[1auc]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1auc' size='340' side='right'caption='[[1auc]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1AUC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUC FirstGlance]. <br>
-	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [~~http~~://pdbe.org/1auc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1auc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1auc ProSAT]</span></td></tr>	+	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [https://pdbe.org/1auc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [https://www.ebi.ac.uk/pdbsum/1auc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>	+	[[https://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 29:

	==See Also==		==See Also==
-	*[[Thioredoxin\|Thioredoxin]]	+	*[[Thioredoxin 3D structures\|Thioredoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:55, 22 January 2020

2020-01-22T17:55:46Z

←Older revision		Revision as of 17:55, 22 January 2020
Line 1:		Line 1:

	==HUMAN THIOREDOXIN (OXIDIZED WITH DIAMIDE)==		==HUMAN THIOREDOXIN (OXIDIZED WITH DIAMIDE)==
-	<StructureSection load='1auc' size='340' side='right' caption='[[1auc]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1auc' size='340' side='right'caption='[[1auc]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
	[[Category: Anderson, J F]]		[[Category: Anderson, J F]]
	[[Category: Gasdaska, J]]		[[Category: Gasdaska, J]]

OCA at 05:55, 18 April 2018

2018-04-18T05:55:09Z

←Older revision		Revision as of 05:55, 18 April 2018
Line 12:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1auc_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1auc_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 27:
	</div>		</div>
	<div class="pdbe-citations 1auc" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1auc" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:16, 22 November 2017

2017-11-22T11:16:10Z

←Older revision		Revision as of 11:16, 22 November 2017
Line 1:		Line 1:
		+
	==HUMAN THIOREDOXIN (OXIDIZED WITH DIAMIDE)==		==HUMAN THIOREDOXIN (OXIDIZED WITH DIAMIDE)==
	<StructureSection load='1auc' size='340' side='right' caption='[[1auc]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1auc' size='340' side='right' caption='[[1auc]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>
-	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://pdbe.org/1auc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum]</span></td></tr>	+	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://pdbe.org/1auc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1auc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1auc" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1auc" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:51, 9 February 2016

2016-02-09T17:51:12Z

←Older revision		Revision as of 17:51, 9 February 2016
Line 15:		Line 15:
	<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=1auc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:35, 11 September 2015

2015-09-11T00:35:49Z

←Older revision		Revision as of 00:35, 11 September 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>
-	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum]</span></td></tr>	+	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://pdbe.org/1auc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 25:
	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 1auc" style="background-color:#fffaf0;"></div>

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

OCA at 08:27, 25 December 2014

2014-12-25T08:27:29Z

←Older revision		Revision as of 08:27, 25 December 2014
Line 5:		Line 5:
	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum]</span></td></tr>		</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:13, 22 December 2014

2014-12-22T11:13:42Z

←Older revision		Revision as of 11:13, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>
-	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum]</span></td></tr>	+	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Anderson, J F.]]	+	[[Category: Anderson, J F]]
-	[[Category: Gasdaska, J.]]	+	[[Category: Gasdaska, J]]
-	[[Category: Montfort, W R.]]	+	[[Category: Montfort, W R]]
-	[[Category: Powis, G.]]	+	[[Category: Powis, G]]
-	[[Category: Sanders, D A.R.]]	+	[[Category: Sanders, D A.R]]
-	[[Category: Weichsel, A.]]	+	[[Category: Weichsel, A]]
	[[Category: Dimer]]		[[Category: Dimer]]
	[[Category: Electron transport]]		[[Category: Electron transport]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Thioredoxin]]		[[Category: Thioredoxin]]

OCA at 08:13, 30 July 2014

2014-07-30T08:13:22Z

←Older revision		Revision as of 08:13, 30 July 2014
Line 1:		Line 1:
-	[[~~Image~~:1auc.~~png\|left~~\|200px]]	+	==HUMAN THIOREDOXIN (OXIDIZED WITH DIAMIDE)==
		+	<StructureSection load='1auc' size='340' side='right' caption='[[1auc]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1auc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUC FirstGlance]. <br>
		+	</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=1auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1auc RCSB], [http://www.ebi.ac.uk/pdbsum/1auc 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/au/1auc_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 ==
		+	Thioredoxins are a group of ca. 12 kDa redox proteins that mediate numerous cytosolic processes in all cells. Human thioredoxin can be exported out of the cell where it has additional functions including the ability to stimulate cell growth. A recent crystal structure determination of human thioredoxin revealed an inactive dimeric form of the protein covalently linked through a disulfide bond involving Cys 73 from each monomer [Weichsel et al. (1996) Structure 4, 735-751]. In the present study, apparent dissociation constants (Kapp) for the noncovalently linked dimers were determined at various pHs using a novel assay in which preformed dimers, but not monomers, were rapidly linked through oxidation (with diamide) of the Cys 73 disulfide bond, and the relative amounts of monomer and dimer were detected by gel filtration. The values obtained were pH-dependent, varying between 6.1 and 166 microM for the pH range of 3.8-8.0, and were consistent with the titration of a single ionizable group having a pKa of 6.5. A similar value was obtained using gel filtration at pH 3.8 (Kapp = 164 microM), and the crystal structure of the diamide-oxidized protein was determined to be nearly identical to that obtained in the absence of diamide. Asp 60 lies in the dimer interface and was found to be responsible for the pH dependence for dimer formation, and therefore must have a pKa elevated by approximately 2.5 pH units. Mutation of Asp 60 to asparagine abolished nearly all of the pH dependence for dimer formation. The crystal structure of the D60N mutant revealed a dimer nearly identical to the wild type, but, surprisingly, it had the Asn 60 side chain rotated out of the dimer interface and replaced with two water molecules. The values obtained for Kapp suggest human thioredoxin may dimerize in vivo and possible roles for such dimers are discussed.

-	~~{{STRUCTURE_1auc\| PDB=1auc \| SCENE= }}~~	+	Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant.,Andersen JF, Sanders DA, Gasdaska JR, Weichsel A, Powis G, Montfort WR Biochemistry. 1997 Nov 18;36(46):13979-88. PMID:9369469<ref>PMID:9369469</ref>

-	~~===HUMAN THIOREDOXIN (OXIDIZED WITH DIAMIDE)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9369469}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1auc]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1AUC OCA].~~	+

	==See Also==		==See Also==
	*[[Thioredoxin\|Thioredoxin]]		*[[Thioredoxin\|Thioredoxin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009369469<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Anderson, J F.]]		[[Category: Anderson, J F.]]