title: Structural feature of bent DNA recognized by HMGB1.
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.
authors: Laboratory of Biophysics, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
authors: Kyoko
authors: K
authors: Furuita
authors: Shunpei
authors: S
authors: Murata
authors: Jun Goo
authors: JG
authors: Jee
authors: Satoshi
authors: S
authors: Ichikawa
authors: Akira
authors: A
authors: Matsuda
authors: Chojiro
authors: C
authors: Kojima
mesh_terms: D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D024243:HMGB1 Protein / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding
chemical_list: D024243:HMGB1 Protein; D004247:DNA