2rtu
From Proteopedia
(Difference between revisions)
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== 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 | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</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]] | ||
Revision as of 21:41, 24 December 2014
Solution structure of oxidized human HMGB1 A box
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