Abstract
The estrogen receptor (ER) is a member of the family of nuclear receptors that has become an important therapeutic target for the treatment of osteoporosis and a variety of cancers. The response of ER to estrogenic ligands is mediated by a wide range of coactivator and corepressor proteins with the NR box sequence motif that binds to helix 12 (H12) of ER. We have studied ER‐coactivator interactions by the spin labeling method, in which a nitroxide reporter group is attached either to H12 or to a peptide sequence containing the NR box. Lineshape analysis of the electron spin resonance (ESR) spectra of such labels allows them to be characterized in terms of local mobility and ordering, providing new physical details about the binding of different coactivator sequences. Research supported by Army BCRP award W81XWH‐06‐1‐0551 and a Merck Undergraduate Summer Research Fellowship.
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