Indentification of sites in oxytocin involved in uterine receptor recognition and activation.

Following a brief review of the preferred three-dimensional structured proposed for oxytocin in dimethylsulfoxide and in aqueous medium, the "cooperative model" for the biologically active conformation of oxytocin is discussed. An approach to conformation-activity analysis is described. The importance of determining the peptide backbone conformation and the functional contribution of peptide backbone and amino acid side chains to hormone receptor interactions are analyzed. Sites are proposed that are thought to be involved in the binding process of oxytocin to the smooth muscle receptor in rat uterus, as well as sites that are thought to be responsible for receptor activation.