4ll1 - Revision history

OCA at 06:50, 3 April 2024

2024-04-03T06:50:04Z

←Older revision		Revision as of 06:50, 3 April 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ll1]] 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=4LL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LL1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ll1]] 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=4LL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LL1 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=4ll1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll1 OCA], [https://pdbe.org/4ll1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ll1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ll1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ll1 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]] 2Å</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=4ll1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll1 OCA], [https://pdbe.org/4ll1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ll1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ll1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ll1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</ref>		[https://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The redox-dependent inhibition of thioredoxin (TRX) by thioredoxin-interacting protein (TXNIP) plays a pivotal role in various cancers and metabolic syndromes. However, the molecular mechanism of this regulation is largely unknown. Here, we present the crystal structure of the TRX-TXNIP complex and demonstrate that the inhibition of TRX by TXNIP is mediated by an intermolecular disulphide interaction resulting from a novel disulphide bond-switching mechanism. Upon binding to TRX, TXNIP undergoes a structural rearrangement that involves switching of a head-to-tail interprotomer Cys63-Cys247 disulphide between TXNIP molecules to an interdomain Cys63-Cys190 disulphide, and the formation of a de novo intermolecular TXNIP Cys247-TRX Cys32 disulphide. This disulphide-switching event unexpectedly results in a domain arrangement of TXNIP that is entirely different from those of other arrestin family proteins. We further show that the intermolecular disulphide bond between TRX and TXNIP dissociates in the presence of high concentrations of reactive oxygen species. This study provides insight into TRX and TXNIP-dependent cellular regulation.
-
-	The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein.,Hwang J, Suh HW, Jeon YH, Hwang E, Nguyen LT, Yeom J, Lee SG, Lee C, Kim KJ, Kang BS, Jeong JO, Oh TK, Choi I, Lee JO, Kim MH Nat Commun. 2014 Jan 6;5:2958. doi: 10.1038/ncomms3958. PMID:24389582<ref>PMID:24389582</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4ll1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:07, 14 December 2022

2022-12-14T11:07:28Z

←Older revision		Revision as of 11:07, 14 December 2022
Line 1:		Line 1:

	==The structure of the TRX and TXNIP complex==		==The structure of the TRX and TXNIP complex==
-	<StructureSection load='4ll1' size='340' side='right' caption='[[4ll1]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4ll1' size='340' side='right'caption='[[4ll1]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ll1]] 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=4LL1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LL1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ll1]] 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=4LL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LL1 FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gfx\|4gfx]], [[4ll4\|4ll4]]</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=4ll1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll1 OCA], [https://pdbe.org/4ll1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ll1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ll1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ll1 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TXNIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TRX ([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=4ll1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll1 OCA], [~~http~~://pdbe.org/4ll1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ll1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ll1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ll1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN]] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</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>	+	[https://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Hwang, J~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Kim, M H~~]]	+	[[Category: Hwang J]]
-	[[Category: ~~Antitumor protein-protein binding complex]]~~	+	[[Category: Kim MH]]
-	~~[[Category: Arrestin-like domain~~]]	+

OCA at 03:04, 5 August 2016

2016-08-05T03:04:16Z

←Older revision		Revision as of 03:04, 5 August 2016
Line 1:		Line 1:
		+
	==The structure of the TRX and TXNIP complex==		==The structure of the TRX and TXNIP complex==
	<StructureSection load='4ll1' size='340' side='right' caption='[[4ll1]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4ll1' size='340' side='right' caption='[[4ll1]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gfx\|4gfx]], [[4ll4\|4ll4]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gfx\|4gfx]], [[4ll4\|4ll4]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TXNIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TRX ([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">TXNIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TRX ([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=4ll1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ll1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ll1 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=4ll1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll1 OCA], [http://pdbe.org/4ll1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ll1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ll1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ll1 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 4ll1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:21, 25 December 2014

2014-12-25T15:21:56Z

←Older revision		Revision as of 15:21, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ll1\| PDB~~=4ll1 \| ~~SCENE~~= }}	+	==The structure of the TRX and TXNIP complex==
-	===~~The~~ structure of the ~~TRX and~~ TXNIP ~~complex~~===	+	<StructureSection load='4ll1' size='340' side='right' caption='[[4ll1]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24389582}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4ll1]] 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=4LL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LL1 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gfx\|4gfx]], [[4ll4\|4ll4]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TXNIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TRX ([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=4ll1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ll1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ll1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ll1 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN]] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</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>		[[http://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN]] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The redox-dependent inhibition of thioredoxin (TRX) by thioredoxin-interacting protein (TXNIP) plays a pivotal role in various cancers and metabolic syndromes. However, the molecular mechanism of this regulation is largely unknown. Here, we present the crystal structure of the TRX-TXNIP complex and demonstrate that the inhibition of TRX by TXNIP is mediated by an intermolecular disulphide interaction resulting from a novel disulphide bond-switching mechanism. Upon binding to TRX, TXNIP undergoes a structural rearrangement that involves switching of a head-to-tail interprotomer Cys63-Cys247 disulphide between TXNIP molecules to an interdomain Cys63-Cys190 disulphide, and the formation of a de novo intermolecular TXNIP Cys247-TRX Cys32 disulphide. This disulphide-switching event unexpectedly results in a domain arrangement of TXNIP that is entirely different from those of other arrestin family proteins. We further show that the intermolecular disulphide bond between TRX and TXNIP dissociates in the presence of high concentrations of reactive oxygen species. This study provides insight into TRX and TXNIP-dependent cellular regulation.

-	~~==About this Structure==~~	+	The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein.,Hwang J, Suh HW, Jeon YH, Hwang E, Nguyen LT, Yeom J, Lee SG, Lee C, Kim KJ, Kang BS, Jeong JO, Oh TK, Choi I, Lee JO, Kim MH Nat Commun. 2014 Jan 6;5:2958. doi: 10.1038/ncomms3958. PMID:24389582<ref>PMID:24389582</ref>
-	~~[[4ll1]] is a 4 chain structure~~. ~~Full crystallographic information is available from [http~~:~~//oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4LL1 OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024389582</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Hwang, J.]]	+	== References ==
-	[[Category: Kim, M H.]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Hwang, J]]
		+	[[Category: Kim, M H]]
	[[Category: Antitumor protein-protein binding complex]]		[[Category: Antitumor protein-protein binding complex]]
	[[Category: Arrestin-like domain]]		[[Category: Arrestin-like domain]]

OCA at 11:23, 5 February 2014

2014-02-05T11:23:17Z

←Older revision		Revision as of 11:23, 5 February 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4ll1\| PDB=4ll1 \| SCENE= }}
		+	===The structure of the TRX and TXNIP complex===
		+	{{ABSTRACT_PUBMED_24389582}}

-	~~The entry 4ll1 is ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN]] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</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>

-	~~Authors~~: ~~Hwang, J~~.~~, Kim, M~~.H.	+	==About this Structure==
		+	[[4ll1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LL1 OCA].

-	~~Description~~: ~~The structure of the TRX and TXNIP~~ complex	+	==Reference==
		+	<ref group="xtra">PMID:024389582</ref><references group="xtra"/><references/>
		+	[[Category: Hwang, J.]]
		+	[[Category: Kim, M H.]]
		+	[[Category: Antitumor protein-protein binding complex]]
		+	[[Category: Arrestin-like domain]]

OCA at 04:18, 1 August 2013

2013-08-01T04:18:23Z

←Older revision		Revision as of 04:18, 1 August 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ll1 is ON HOLD	+	The entry 4ll1 is ON HOLD until Paper Publication

	Authors: Hwang, J., Kim, M.H.		Authors: Hwang, J., Kim, M.H.

	Description: The structure of the TRX and TXNIP complex		Description: The structure of the TRX and TXNIP complex

OCA: Protected "4ll1" [edit=sysop:move=sysop]

2013-07-18T04:47:35Z

Protected "4ll1" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:47, 18 July 2013

OCA: New page: '''Unreleased structure''' The entry 4ll1 is ON HOLD Authors: Hwang, J., Kim, M.H. Description: The structure of the TRX and TXNIP complex

2013-07-18T04:47:34Z

New page: '''Unreleased structure''' The entry 4ll1 is ON HOLD Authors: Hwang, J., Kim, M.H. Description: The structure of the TRX and TXNIP complex

New page

'''Unreleased structure'''

The entry 4ll1 is ON HOLD

Authors: Hwang, J., Kim, M.H.

Description: The structure of the TRX and TXNIP complex