4oo4 - Revision history

OCA at 17:17, 20 September 2023

2023-09-20T17:17:10Z

←Older revision		Revision as of 17:17, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4oo4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OO4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4oo4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OO4 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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [https://pdbe.org/4oo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [https://www.ebi.ac.uk/pdbsum/4oo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oo4 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]] 0.97Å</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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [https://pdbe.org/4oo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [https://www.ebi.ac.uk/pdbsum/4oo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oo4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 07:35, 25 January 2023

2023-01-25T07:35:10Z

←Older revision		Revision as of 07:35, 25 January 2023
Line 1:		Line 1:

	==Crystal Structure of Human Thioredoxin Mutant==		==Crystal Structure of Human Thioredoxin Mutant==
-	<StructureSection load='4oo4' size='340' side='right' caption='[[4oo4]], [[Resolution\|resolution]] 0.97Å' scene=''>	+	<StructureSection load='4oo4' size='340' side='right'caption='[[4oo4]], [[Resolution\|resolution]] 0.97Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4oo4]] is a 2 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=4OO4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4OO4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4oo4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OO4 FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m9j\|3m9j]], [[3m9k\|3m9k]], [[4oo5\|4oo5]]</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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [https://pdbe.org/4oo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [https://www.ebi.ac.uk/pdbsum/4oo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oo4 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TXN, TRDX, TRX, TRX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [~~http~~://pdbe.org/4oo4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4oo4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4oo4 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>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Thioredoxins reduce disulfide bonds and other thiol modifications in all cells, using a CXXC motif. Human thioredoxin 1 is unusual in that it codes for an additional three cysteines in its 105 amino acid sequence, each of which have been implicated in other reductive activities. Cys 62 and Cys 69 are buried in the protein interior and lie at either end of a short helix (helix 3), and yet can disulfide link under oxidizing conditions. Cys 62 is readily S-nitrosated, giving rise to a SNO modification, which is also buried. Here, we present two crystal structures of the C69S/C73S mutant protein under oxidizing (1.5 A) and reducing (1.1 A) conditions. In the oxidized structure, helix 3 is unraveled and displays a new conformation that is stabilized by a series of new hydrogen bonds and a disulfide link with Cys 62 in a neighboring molecule. The new conformation provides an explanation for how a completely buried residue can participate in SNO exchange reactions.	+
-		+
-	~~Crystal structure of human thioredoxin revealing an unraveled helix and exposed S- nitrosation site.,Weichsel A, Kem M, Montfort WR Protein Sci. 2010 Jul 26. PMID:20662007<ref>PMID:20662007</ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4oo4" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
-	*[[Thioredoxin\|Thioredoxin]]	+	*[[Thioredoxin 3D structures\|Thioredoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Montfort, W R~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~The, J~~]]	+	[[Category: Montfort WR]]
-	[[Category: ~~Weichsel, A~~]]	+	[[Category: The J]]
-	[[Category: ~~Oxidoreductase]]~~	+	[[Category: Weichsel A]]
-	~~[[Category: S-nitrosation~~]]	+

OCA at 13:14, 4 August 2016

2016-08-04T13:14:34Z

←Older revision		Revision as of 13:14, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Human Thioredoxin Mutant==		==Crystal Structure of Human Thioredoxin Mutant==
	<StructureSection load='4oo4' size='340' side='right' caption='[[4oo4]], [[Resolution\|resolution]] 0.97Å' scene=''>		<StructureSection load='4oo4' size='340' side='right' caption='[[4oo4]], [[Resolution\|resolution]] 0.97Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m9j\|3m9j]], [[3m9k\|3m9k]], [[4oo5\|4oo5]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m9j\|3m9j]], [[3m9k\|3m9k]], [[4oo5\|4oo5]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TXN, TRDX, TRX, TRX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TXN, TRDX, TRX, TRX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oo4 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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [http://pdbe.org/4oo4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oo4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oo4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4oo4" style="background-color:#fffaf0;"></div>

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

OCA at 09:37, 25 December 2014

2014-12-25T09:37:50Z

←Older revision		Revision as of 09:37, 25 December 2014
Line 7:		Line 7:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oo4 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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oo4 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 04:41, 22 December 2014

2014-12-22T04:41:49Z

←Older revision		Revision as of 04:41, 22 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4oo4\| PDB~~=4oo4 \| ~~SCENE~~= }}	+	==Crystal Structure of Human Thioredoxin Mutant==
-	===~~Crystal Structure of~~ Human ~~Thioredoxin Mutant~~===	+	<StructureSection load='4oo4' size='340' side='right' caption='[[4oo4]], [[Resolution\|resolution]] 0.97Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20662007}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4oo4]] is a 2 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=4OO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OO4 FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3m9j\|3m9j]], [[3m9k\|3m9k]], [[4oo5\|4oo5]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TXN, TRDX, TRX, TRX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oo4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oo4 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Thioredoxins reduce disulfide bonds and other thiol modifications in all cells, using a CXXC motif. Human thioredoxin 1 is unusual in that it codes for an additional three cysteines in its 105 amino acid sequence, each of which have been implicated in other reductive activities. Cys 62 and Cys 69 are buried in the protein interior and lie at either end of a short helix (helix 3), and yet can disulfide link under oxidizing conditions. Cys 62 is readily S-nitrosated, giving rise to a SNO modification, which is also buried. Here, we present two crystal structures of the C69S/C73S mutant protein under oxidizing (1.5 A) and reducing (1.1 A) conditions. In the oxidized structure, helix 3 is unraveled and displays a new conformation that is stabilized by a series of new hydrogen bonds and a disulfide link with Cys 62 in a neighboring molecule. The new conformation provides an explanation for how a completely buried residue can participate in SNO exchange reactions.

-	~~==Function==~~	+	Crystal structure of human thioredoxin revealing an unraveled helix and exposed S- nitrosation site.,Weichsel A, Kem M, Montfort WR Protein Sci. 2010 Jul 26. PMID:20662007<ref>PMID:20662007</ref>
-	~~[[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>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4oo4]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4OO4 OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:020662007</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Thioredoxin\|Thioredoxin]]
-	[[Category: Montfort, W R.]]	+	== References ==
-	[[Category: The, J.]]	+	<references/>
-	[[Category: Weichsel, A.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Montfort, W R]]
		+	[[Category: The, J]]
		+	[[Category: Weichsel, A]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: S-nitrosation]]		[[Category: S-nitrosation]]

OCA at 05:09, 13 February 2014

2014-02-13T05:09:27Z

←Older revision		Revision as of 05:09, 13 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4oo4\| PDB=4oo4 \| SCENE= }}
		+	===Crystal Structure of Human Thioredoxin Mutant===
		+	{{ABSTRACT_PUBMED_20662007}}

-	~~The entry 4oo4 is ON HOLD~~	+	==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>

-	~~Authors~~: ~~The, J~~.~~, Weichsel, A~~.~~, Montfort, W~~.R.	+	==About this Structure==
		+	[[4oo4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OO4 OCA].

-	~~Description~~: ~~Crystal Structure of Human Thioredoxin Mutant~~	+	==Reference==
		+	<ref group="xtra">PMID:020662007</ref><references group="xtra"/><references/>
		+	[[Category: Montfort, W R.]]
		+	[[Category: The, J.]]
		+	[[Category: Weichsel, A.]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: S-nitrosation]]

OCA: Protected "4oo4" [edit=sysop:move=sysop]

2014-02-05T10:35:40Z

Protected "4oo4" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:35, 5 February 2014

OCA: New page: '''Unreleased structure''' The entry 4oo4 is ON HOLD Authors: The, J., Weichsel, A., Montfort, W.R. Description: Crystal Structure of Human Thioredoxin Mutant

2014-02-05T10:35:39Z

New page: '''Unreleased structure''' The entry 4oo4 is ON HOLD Authors: The, J., Weichsel, A., Montfort, W.R. Description: Crystal Structure of Human Thioredoxin Mutant

New page

'''Unreleased structure'''

The entry 4oo4 is ON HOLD

Authors: The, J., Weichsel, A., Montfort, W.R.

Description: Crystal Structure of Human Thioredoxin Mutant