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Journal of Biomolecular Screening
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Article

Peptide Binding Identifies an ER{alpha} Conformation That Generates Selective Activity in Multiple In Vitro Assays

Christopher J. Larson, Deborah L. Osburn, Katherine Schmitz, Leslie Giampa, Shau-Ming Mong, Keith Marschke, H. Martin Seidel, Jonathan Rosen*, Andrés Negro-Vilar

Departments of Molecular & Cell Biology and New Leads Discovery Ligand Pharmaceuticals, San Diego, CA.

* To whom correspondence should be addressed. E-mail: jrosen{at}ligand.com.


  Abstract

Drugs such as tamoxifen, which act at the estrogen receptor (ER), have very different in vitro and in vivo effects from those of the native hormone. Previous research has established that different ligands induce distinct conformational changes in the ER, thus affecting the interactions of the receptor with cell-specific coactivating or corepressing proteins (cofactors) and estrogen response elements (EREs), thus potentially driving differing biological effects. Affinity-selected peptides have been used to probe the conformational changes that occur within the ER upon binding various ligands. In this study, the authors characterize the ability of several peptides to be recruited to liganded ER under cellular conditions. Approximating ER conformation via recruitment of this peptide to the ER is concluded to be a better predictor of the agonist nature of an ER ligand under these different cellular contexts than is a canonical cotransfection transactivation assay.

Key Words: agonism, Gal4 DNA-binding domain, ligand-binding domain, nuclear receptor, selective estrogen receptor modulator

First published on August 15, 2005, doi:10.1177/1087057105275983

Journal of Biomolecular Screening 2005;10:590.

A more recent version of this article appeared on September 1, 2005

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