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To interrogate the relative importance of consensus structure interactions for receptor binding and activation, we employed receptor mutagenesis, where each residue within the TMD that formed an interaction with any of the four peptides in the static cryo-EM structures was mutated to alanine (with the exception of A368 6.57 , which was mutated to glycine), and the binding affinity and cAMP signalling of each peptide was assessed

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