2rtu - Revision history

OCA at 08:39, 30 October 2024

2024-10-30T08:39:47Z

← Older revision		Revision as of 08:39, 30 October 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RTU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RTU 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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [https://pdbe.org/2rtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [https://www.ebi.ac.uk/pdbsum/2rtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rtu ProSAT]</span></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [https://pdbe.org/2rtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [https://www.ebi.ac.uk/pdbsum/2rtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rtu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 10:04, 14 June 2023

2023-06-14T10:04:11Z

← Older revision		Revision as of 10:04, 14 June 2023
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	==Solution structure of oxidized human HMGB1 A box==		==Solution structure of oxidized human HMGB1 A box==
	<StructureSection load='2rtu' size='340' side='right'caption='[[2rtu~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>		<StructureSection load='2rtu' size='340' side='right'caption='[[2rtu]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RTU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RTU FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMGB1, HMG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [https://pdbe.org/2rtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [https://www.ebi.ac.uk/pdbsum/2rtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rtu 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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [https://pdbe.org/2rtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [https://www.ebi.ac.uk/pdbsum/2rtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rtu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/HMGB1_HUMAN HMGB1_HUMAN]] DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity).		[https://www.uniprot.org/uniprot/HMGB1_HUMAN HMGB1_HUMAN] DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Jing, W]]		[[Category: Jing W]]
	[[Category: Tate, S]]		[[Category: Tate S]]
	[[Category: Tochio, N]]		[[Category: Tochio N]]
	~~[[Category: Disulfide bond]]~~
	~~[[Category: Dna binding protein]]~~
	~~[[Category: High mobility group box 1~~]]

OCA at 20:54, 20 October 2021

2021-10-20T20:54:40Z

← Older revision		Revision as of 20:54, 20 October 2021
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	<StructureSection load='2rtu' size='340' side='right'caption='[[2rtu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rtu' size='340' side='right'caption='[[2rtu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2RTU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RTU FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMGB1, HMG1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMGB1, HMG1 ([https://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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [~~http~~://pdbe.org/2rtu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2rtu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2rtu 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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [https://pdbe.org/2rtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [https://www.ebi.ac.uk/pdbsum/2rtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rtu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/HMGB1_HUMAN HMGB1_HUMAN]] DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity).		[[https://www.uniprot.org/uniprot/HMGB1_HUMAN HMGB1_HUMAN]] DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 22:56, 5 June 2019

2019-06-05T22:56:44Z

← Older revision		Revision as of 22:56, 5 June 2019
Line 1:		Line 1:

	==Solution structure of oxidized human HMGB1 A box==		==Solution structure of oxidized human HMGB1 A box==
	<StructureSection load='2rtu' size='340' side='right' caption='[[2rtu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rtu' size='340' side='right'caption='[[2rtu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RTU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RTU FirstGlance]. <br>
Line 13:		Line 13:
	HMGB1 (high-mobility group B1) is a ubiquitously expressed bifunctional protein that acts as a nuclear protein in cells and also as an inflammatory mediator in the extracellular space. HMGB1 changes its functions according to the redox states in both intra- and extra-cellular environments. Two cysteines, Cys23 and Cys45, in the A-domain of HMGB1 form a disulfide bond under oxidative conditions. The A-domain with the disulfide bond shows reduced affinity to cisplatin modified DNA. We have solved the oxidized A-domain structure by NMR. In the structure, Phe38 has a flipped ring orientation from that found in the reduced form; the phenyl ring in the reduced form intercalates into the platinated lesion in DNA. The phenyl ring orientation in the oxidized form is stabilized through intramolecular hydrophobic contacts. The reorientation of the Phe38 ring by the disulfide bond in the A-domain may explain the reduced HMGB1 binding affinity towards cisplatinated DNA.		HMGB1 (high-mobility group B1) is a ubiquitously expressed bifunctional protein that acts as a nuclear protein in cells and also as an inflammatory mediator in the extracellular space. HMGB1 changes its functions according to the redox states in both intra- and extra-cellular environments. Two cysteines, Cys23 and Cys45, in the A-domain of HMGB1 form a disulfide bond under oxidative conditions. The A-domain with the disulfide bond shows reduced affinity to cisplatin modified DNA. We have solved the oxidized A-domain structure by NMR. In the structure, Phe38 has a flipped ring orientation from that found in the reduced form; the phenyl ring in the reduced form intercalates into the platinated lesion in DNA. The phenyl ring orientation in the oxidized form is stabilized through intramolecular hydrophobic contacts. The reorientation of the Phe38 ring by the disulfide bond in the A-domain may explain the reduced HMGB1 binding affinity towards cisplatinated DNA.

	Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.,Wang J, Tochio N, Takeuchi A, Uewaki JI, Kobayashi N, Tate SI Biochem Biophys Res Commun. 2013 ~~Oct 25. pii: S0006-291X~~(13)~~01766~~-~~X. doi:, 10.1016/j.bbrc.2013.10.085~~. PMID:~~24513216~~<ref>PMID:~~24513216~~</ref>		Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.,Wang J, Tochio N, Takeuchi A, Uewaki J, Kobayashi N, Tate S Biochem Biophys Res Commun. 2013 Nov 29;441(4):701-6. PMID:24427810<ref>PMID:24427810</ref>

	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>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Jing, W]]		[[Category: Jing, W]]
	[[Category: Tate, S]]		[[Category: Tate, S]]

OCA at 01:41, 5 August 2016

2016-08-05T01:41:06Z

← Older revision		Revision as of 01:41, 5 August 2016
Line 1:		Line 1:

	==Solution structure of oxidized human HMGB1 A box==		==Solution structure of oxidized human HMGB1 A box==
	<StructureSection load='2rtu' size='340' side='right' caption='[[2rtu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2rtu' size='340' side='right' caption='[[2rtu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RTU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RTU FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMGB1, HMG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMGB1, HMG1 ([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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [http://www.ebi.ac.uk/pdbsum/2rtu 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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [http://pdbe.org/2rtu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [http://www.ebi.ac.uk/pdbsum/2rtu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rtu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 2rtu" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[High mobility group protein\|High mobility group protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:41, 24 December 2014

2014-12-24T21:41:30Z

← Older revision		Revision as of 21:41, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RTU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2rtu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RTU FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMGB1, HMG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">HMGB1, HMG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [http://www.ebi.ac.uk/pdbsum/2rtu 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=2rtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rtu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rtu RCSB], [http://www.ebi.ac.uk/pdbsum/2rtu PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/HMGB1_HUMAN HMGB1_HUMAN]] DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.,Wang J, Tochio N, Takeuchi A, Uewaki JI, Kobayashi N, Tate SI Biochem Biophys Res Commun. 2013 Oct 25. pii: S0006-291X(13)01766-X. doi:, 10.1016/j.bbrc.2013.10.085. PMID:24513216<ref>PMID:24513216</ref>		Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.,Wang J, Tochio N, Takeuchi A, Uewaki JI, Kobayashi N, Tate SI Biochem Biophys Res Commun. 2013 Oct 25. pii: S0006-291X(13)01766-X. doi:, 10.1016/j.bbrc.2013.10.085. PMID:24513216<ref>PMID:24513216</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 19:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
	[[Category: Jing, W.]]		[[Category: Jing, W]]
	[[Category: Tate, S.]]		[[Category: Tate, S]]
	[[Category: Tochio, N.]]		[[Category: Tochio, N]]
	[[Category: Disulfide bond]]		[[Category: Disulfide bond]]
	[[Category: Dna binding protein]]		[[Category: Dna binding protein]]
	[[Category: High mobility group box 1]]		[[Category: High mobility group box 1]]

OCA at 11:46, 18 May 2014

2014-05-18T11:46:12Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Solution structure of oxidized human HMGB1 A box==
-The entry 2rtu is ON HOLD  until Paper Publication
+Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.,Wang J, Tochio N, Takeuchi A, Uewaki JI, Kobayashi N, Tate SI Biochem Biophys Res Commun. 2013 Oct 25. pii: S0006-291X(13)01766-X. doi:, 10.1016/j.bbrc.2013.10.085. PMID:24513216<ref>PMID:24513216</ref>
-Authors: Jing, W., Tochio, N., Tate, S.
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Solution structure of oxidized human HMGB1 A box
+== References ==

OCA at 05:29, 23 October 2013

2013-10-23T05:29:52Z

← Older revision		Revision as of 05:29, 23 October 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 2rtu is ON HOLD		The entry 2rtu is ON HOLD until Paper Publication

	Authors: Jing, W., Tochio, N., Tate, S.		Authors: Jing, W., Tochio, N., Tate, S.

	Description: Solution structure of oxidized human HMGB1 A box		Description: Solution structure of oxidized human HMGB1 A box

OCA at 05:21, 10 October 2013

2013-10-10T05:21:16Z

← Older revision		Revision as of 05:21, 10 October 2013
Line 5:		Line 5:
	Authors: Jing, W., Tochio, N., Tate, S.		Authors: Jing, W., Tochio, N., Tate, S.

	Description: ~~solution~~ structure of oxidized human HMGB1 A box		Description: Solution structure of oxidized human HMGB1 A box

OCA: Protected "2rtu" [edit=sysop:move=sysop]

2013-09-20T03:11:20Z

Protected "2rtu" [edit=sysop:move=sysop]

← Older revision	Revision as of 03:11, 20 September 2013
(No difference)