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. 2000 Aug;1(2):109-14.
doi: 10.1093/embo-reports/kvd030.

Upwardly mobile proteins. Workshop: the role of HMG proteins in chromatin structure, gene expression and neoplasia

M E Bianchi  1 , M Beltrame
Affiliations

Upwardly mobile proteins. Workshop: the role of HMG proteins in chromatin structure, gene expression and neoplasia

M E Bianchi et al. EMBO Rep. 2000 Aug.
No abstract available

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Figures

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Fig. 1. Structure of AT-hooks and HMG boxes, as determined by the laboratory of M. Clore (Bethesda, MD). (A) The second AT-hook domain of the HMG-I(Y) protein (purple) is bound to the minor groove of a synthetic DNA substrate (yellow); polar view down the long axis of the double helix. The side-chains of the highly conserved arginine residues that form a planar crescent-shaped structure similar in shape to the drugs distamycin and netropsin are also depicted. (B) The HMG box of human SRY (magenta) bound to the minor groove of the octanucleotide GCACAAAC. HMG boxes are composed of three α-helices and an extended amino acid stretch at their N-terminus. The backbones of the HMG box domains of SRY, HMG1 and Drosophila HMG-D are almost exactly superimposable. The DNA (yellow) is significantly distorted: the minor groove is widened considerably to accommodate the extended N-terminal stretch of the HMG box; the planes of the bases are tilted; and the double helix is unwound and bent.
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