The structure of the hormone-receptor interface for hLH/CG receptor was examined to identify potential small molecule antagonists or agonists that act on the receptor. Two parallel yet complementary sets of experiments were initiated. Firstly, the production and purification of large quantities of the extracellular binding domain of hLH/CG receptor to be used for crystallographic studies. Preparative quantities of properly folded extracellular domain of hLH/CG receptor as a fusion protein in a prokaryotic based system is being utilized for growing crystals for diffraction studies. The second approach involves a small molecule screen based analysis of the binding domain of hLH/CG receptor. This technique is being utilized to map the molecular surface of the receptor-ligand interface of hLH/CG receptor by identifying specific small molecule antagonists and/or agonists, defining the functional moieties responsible for their activities and examining the bound or "docked" conformation of these molecules with the receptor. These studies offer a more rapid analysis of the receptor-ligand interface and identification of small molecules that act on the receptor. The progress with these latter studies and the potential of this approach are discussed in detail in this review.
|Number of pages||13|
|Journal||Indian Journal of Experimental Biology|
|State||Published - 1 Jan 2002|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology