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The structure and structural properties of nuclear receptors is described focusing on the ligand-binding and DNA binding domains and unstructured N-terminal regions. To emphasize the allosteric interdependence among these subunits, a more detailed inspection of the structural properties of the human progesterone receptor is presented.

A quantitative analysis of progesterone receptor (PR)-B self-association energetics is conducted. The studies highlight questions about the relative roles of monomer and dimer in PR-dependent biological function and may additionally offer insight into the mechanisms by which closely related steroid receptors generate transcriptional diversity.

Ketalization of the biomolecule progesterone with (6-bromo-7-hydroxycoumarin-4-yl)ethane-1,2-diol has given the photolabile progesterone derivatives and has displayed reduced bioactivity and release progesterone upon irradiation with ultraviolet/visible or infrared light. The utility of the derivative is shown by measurement of changes in swimming behavior of single human sperm caused by progesterone-induced [Ca.sup.2+]-influx in the sperm flagellum.

The design of a new class of potential nonsteroidal human progesterone receptor (hPR) inhibitors based on the molecular modeling and QSAR analysis of the known hPR inhibitor Mifepristone (RU-486) and other hPR ligands is reported. The key step in the process involves a stereoselective epoxide ring opening and the reductive Heck cyclization to form the main framework of racemic compound.

The study of Tpr2, also called DjC7, a TPR domain-containing type III J protein implicated in steroid receptor chaperoning is reported. The results showed that Tpr2 promoted the accumulation of the molecular chaperones Hsp70 in progesterone receptor (PR) heterocomplexes in the presence of Hsp90.

A novel site for tetratricopeptide (TPR) cochaperone interaction at the N-terminal and C-terminal ATP binding domain of Hsp90 is described. The results provide insight into two proteins, GCUNC45 and FKBP52, which assist progesterone receptor chaperoning and interact sequentially with PR-Hsp90 complexes.