Structural feature of bent DNA recognized by HMGB1.

Authors :: Furuita K
Murata S
Jee JG
Ichikawa S
Matsuda A
Kojima C
Source :: Journal of the American Chemical Society [J Am Chem Soc] 2011 Apr 20; Vol. 133 (15), pp. 5788-90. Date of Electronic Publication: 2011 Mar 28.
Publication Year :: 2011
Abstract: 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.