View source for 2rtu


==Solution structure of oxidized human HMGB1 A box==
<StructureSection load='2rtu' size='340' side='right'caption='[[2rtu]]' scene=''>
== 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>
</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>
== 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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 J, Kobayashi N, Tate S Biochem Biophys Res Commun. 2013 Nov 29;441(4):701-6. PMID:24427810<ref>PMID:24427810</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rtu" style="background-color:#fffaf0;"></div>

==See Also==
*[[High mobility group protein|High mobility group protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Jing W]]
[[Category: Tate S]]
[[Category: Tochio N]]