Modulation of nuclear receptor interactions by ligands: kinetic analysis using surface plasmon resonance

Biochemistry
B Cheskis, L P Freedman

Abstract

Many nuclear hormone receptors, including the human 1,25-dihydroxyvitamin D3 receptor (VDR), bind cooperatively to DNA as either homodimers or heterodimers with the 9-cis-retinoic acid receptor (RXR). Protein-protein interactions mediated by residues within both the DNA- and ligand-binding domains contribute to this binding. We have previously reported that the ligands for VDR and RXR can modulate the affinity of the receptors' interaction with DNA [Cheskis, B., & Freedman, L. P. (1994) Mol. Cell. Biol. 14, 3329-3338]. To examine this in more detail, we report here the use of surface plasmon resonance (SPR) to characterize the kinetics of both protein-protein and protein-DNA interactions by VDR and RXR in the presence and absence of their cognate ligands. We find that 1,25 dihydroxyvitamin D3 binding favors both VDR-RXR heterodimerization and, as a result, DNA binding by the complex. Conversely, the ligand reduces VDR homodimerization in solution and the affinity of VDR-DNA interaction. 9-cis-Retinoic acid attenuates the stimulating effect of 1,25-dihydroxyvitamin D3 by decreasing the rate of VDR-RXR heterodimer formation and simultaneously by increasing the affinity of RXR homodimerization. Thus, using SPR, we have shown that ...Continue Reading

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Citations

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