The solution structure of an HMG-I(Y)–DNA complex defines a new architectural minor groove binding motif

@article{Huth1997TheSS,
  title={The solution structure of an HMG-I(Y)–DNA complex defines a new architectural minor groove binding motif},
  author={Jeffrey R. Huth and Carole A. Bewley and Mark S. Nissen and Jeremy N. S. Evans and Raymond Reeves and Angela M. Gronenborn and G. Marius Clore},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={657-665}
}
The solution structure of a complex between a truncated form of HMG-I(Y), consisting of the second and third DNA binding domains (residues 51–90), and a DNA dodecamer containing the PRDII site of the interferon-β promoter has been solved by multidimensional nuclear magnetic resonance spectroscopy. The stoichiometry of the complex is one molecule of HMG-I(Y) to two molecules of DNA. The structure reveals a new architectural minor groove binding motif which stabilizes B-DNA, thereby facilitating… 
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The molecular models showed that 1:1 and 2:1 complex formation is driven by the capacity of the ATHPs to bind to the minor and major grooves of the AT-rich DNA oligomers, and complementary solution ITC results confirmed that the2:1 stoichiometry of ATHP: DNA is originated under native conditions in solution.
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