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Therefore, overall exendin-P5 forms relatively stable interactions with the ECD, the upper portion of TM1, TM2 and TM7, and with ECL1 and ECL2, however interactions with key residues deeper in TM2, TM3, TM5, TM6, TM7, as well as with ECL3, are transient, the majority of them present for 75% of the MD simulation in at least one system revealed conserved interactions that were used by all peptides, consistent with a conserved mechanism of signal transmission from the peptide binding site to the G protein binding site (Supplementary Fig

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