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In both peptides, the N-terminal histidine sits in an enclosed pocket forming hydrophobic and hydrogen bond interactions with E364 6 .53 , E387 7 .42 , R310 5 .40 , Y241 3 .44 , W306 5 .36 , I313 5 .43 and Q234 3 .37 however, these interactions are more persistent with GLP-1, and this is likely linked to the stability of interactions of Glu9 and with residues at the base of the binding cavity (Supplemental Table 3, Supplemental Movie 1)

Biomedicines 10(11):2893

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