The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila melanogaster.

@article{Jones1994TheSS,
  title={The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila melanogaster.},
  author={David N. M. Jones and M. Alexandra Searles and Greg L. Shaw and Mair E. A. Churchill and Sarbjit S. Ner and James P. Keeler and Andrew Travers and David Neuhaus},
  journal={Structure},
  year={1994},
  volume={2 7},
  pages={609-27}
}
BACKGROUND The HMG-box is a conserved DNA-binding motif that has been identified in many high mobility group (HMG) proteins. HMG-D is a non-histone chromosomal protein from Drosophila melanogaster that is closely related to the mammalian HMG-box proteins HMG-1 and HMG-2. Previous structures determined for an HMG-box domain from rat and hamster exhibit the same global topology, but differ significantly in detail. It has been suggested that these differences may arise from hinge motions which… CONTINUE READING

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