2rrr

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 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrr OCA], [https://pdbe.org/2rrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrr RCSB], [https://www.ebi.ac.uk/pdbsum/2rrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrr ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-High Mobility Group Box 1 (HMGB1) protein, a potential therapeutic target, binds bent DNAs structure-specifically. Here we report on a crucial structural feature of the bent DNA required for strong binding to HMGB1. NMR structures of two bent DNA oligomers, only one of which binds strongly to HMGB1, revealed that the presence of a pocket structure on the minor groove is crucial for strong binding through penetration of a phenylalanine residue.
-Structural feature of bent DNA recognized by HMGB1.,Furuita K, Murata S, Jee JG, Ichikawa S, Matsuda A, Kojima C J Am Chem Soc. 2011 Apr 20;133(15):5788-90. Epub 2011 Mar 28. PMID:21443191<ref>PMID:21443191</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2rrr" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>