Abstract
The role of Coulombic interactions (1,2,3,4) in the selectivity of DynA fragments toward the ic receptor was investigated by the construction of several rd8 receptor chimeras. The affinity of different Dyn fragments to these chimeric as well as wild type receptors were determined by competition study. Based on the binding profile of DynA fragments at different receptors, it is suggested that while the 8 receptor may contain a high affinity pocket for the Tyr-Gly-Gly-Phe opioid core, the Coulombic interactions between the positive charges in the Dyn peptides and the negative charges in the extracellular (EC) domains of the 1< receptor may play an important role in the selectivity of DynA toward the ic receptor. Restriction sites Aft3 and Bgl2 present in both the rat ~c and 8 receptor cDNA (4, 5) were utilized to produce chimeric 1¢/8 receptors as illustrated in the following figure. Small circles represent the net negative charges in the EC domains.
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