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The Gs heterotrimer engages with the receptor through the same interface observed in peptide-agonist structures, with the alpha-5 helix of Gs-alpha inserting into the intracellular cavity and making contacts with TM3, TM5, TM6, and intracellular loop 2 (ICL2)

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However, the relatively small differences with exendin-asp3 suggest that additional mechanisms beyond receptor trafficking may be involved in the blunted insulin secretory response with this compound