Monomethylarsenite competes with Zn2+ for binding sites in the glucocorticoid receptor

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Department of Chemistry, Dartmouth College, Hanover, NH 03755, United States [1 ]
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Journal of the American Chemical Society | 2008年 / 130卷 / 26期
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The binding of arsenite (As(III)) and monomethylarsenite (MMAIII) to the DNA-binding domain of the glucocorticoid receptor (GR-DBD) and their competition with the two required Zn2+ ions of this domain have been investigated with isothermal titration calorimetry (ITC) and circular dichroism (CD). The binding thermodynamics indicate that MMAIII; but not arsenite; is able to compete with one of the two Zn2+ ions. This has been confirmed by monitoring arsenite and MMAIII titrations of Zn2GR-DBD with CD. Only MMAIII is able to eliminate the Zn-stabilized secondary structure; consistent with partial or complete displacement of at least one Zn2+ ion and; therefore; loss of GR-DBD competence to bind to the DNA of its recognition site; the glucocorticoid response element (GRE). Copyright © 2008 American Chemical Society;
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页码：8148 / 8149
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