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. Author manuscript; available in PMC: 2009 Feb 1.
Published in final edited form as: J Pharmacol Exp Ther. 2007 Nov 15;324(2):463–474. doi: 10.1124/jpet.107.132332

Figure 2.

Figure 2

Affinities of peptides#2-4 for wild-type GRPR, extracellular chimeric GRPRs, and wild-type BRS-3 expressed in CHOP cells (gain-of-affinity chimeras). Diagrams of the chimeric receptors formed are shown at the top. The chimeric GRPRs were formed by replacing each of the extracellular domains of GRPR by the comparable domain of BRS-3 one at a time. Results are expressed as the percentage of the saturable binding seen with no peptide#2-4 present that occurred when the indicated concentration of peptide#2–4 was present. Each point is the mean from at least 5 separate experiments, and in each experiment each point was measured in duplicate. EC2-, e3-, and e4-BRS-3 refer to the substitution of this extracellular domain of BRS-3 for the comparable extracellular domain in GRPR. The arrows indicate large changes in affinity from the wild-type GRPR.