Abstract
The PTH/PTHrP receptor belongs to a novel family of G protein-coupled receptors. Its complex gene spans about 25 kb of genomic DNA, and contains fourteen coding and at least three non-coding exons. Rat and opossum PTH/PTHrP receptors share 78% amino-acid identity, and 91% of the residues are identical when comparing the rat and human receptor homologs. Despite this significant structual conservation, the receptors display distinct functional characteristics when tested with either [Arg2, Tyr34]hPTH (1-34) amide or [Nle8, 18, Tyr34]bPTH (7-34) amide. The construction of chimeras between rat/opossum and between rat/human PTH/PTHrP receptors, and their evaluation with both PTH analogs led to the identification of receptor residues that appear to be involved in ligand/receptor interaction and receptor activation, respectively.
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