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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