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Receptor interactions for the remaining residues within the N-terminal 11 amino acids of exendin-4 were similar to those formed by GLP-1, albeit overall interactions deeper within TM2, TM3, TM5, and ECL2 were generally less persistent, and those in TM1 and TM7 were more persistent (Fig

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SrinivasanSSureshSChendilnathanCPrakashVJSivaprasadSRajalakshmiRet al