THE INTERACTION OF CLASS-B G-PROTEIN-COUPLED RECEPTORS WITH THEIR HORMONES

In common with many G protein-coupled receptors, dysfunction in member s of the Class B or glucagon-like receptors can elicit a wide spectrum of disease related activities. Consequently, they an potential target s in many different areas of pharmacological research. Unlike the clas s A or rhodopsin-like receptors, for which at least some structural si milarity to bacteriorhodopsin has been detected, absolutely no structu ral information is available for the Class B G protein-coupled recepto rs, We present a computational study that exploits the experimental wo rk performed by evolution to indicate residues that are potentially in volved in ligand binding in the Class B G protein-coupled receptors. W e perform an analysis of mutations that occurred in a correlated fashi on between the receptors and their peptidic ligands, The inference tha t the residues detected in this manner are involved in a direct intera ction between the receptor and the ligand is in good agreement with th e mutation studies that have already been published.