Structural feature of bent DNA recognized by HMGB1 |
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| Authors: | Furuita Kyoko Murata Shunpei Jee Jun Goo Ichikawa Satoshi Matsuda Akira Kojima Chojiro |
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| Institution: | Laboratory of Biophysics, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan. |
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| 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. |
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