Ligand binding structure-function relationships

Many hydrophobic molecules such as vitamin A, vitamin D and steroid hormones play vital roles in a variety of cellular processes. Because of the low solubility of these molecules in water, it has been difficult to measure the binding properties of the site-directed mutants of the proteins that interact with these hydrophobic ligands such as cellular retinoic acid binding proteins (CRABPs) (Zhang et al. 1992 Chen et al. 1995). This has greatly hampered the studies of the quantitative structure-function relationships of these important proteins. 

Gold, N. D. and Jackson, R M. (2006) A searchable database for comparing protein-ligand binding sites for the analysis of structure-function relationships. J. Chem. Inf. Model. 46, 736-742. 

Identifying the region of the molecule involved in the direct transmission of allosteric effects is clearly important for understanding how allosteric transitions might be manipulated for therapeutic purposes, particularly if one wished to block an allosteric transition. Understanding the structure-function relationships of the ligands binding to their various sites in an allosteric protein is also critically important. For a homotropic interaction... 

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