Despite the flexibility within the N-terminal two residues, Glu3 of exendin-4 formed very similar contacts to that of Glu9 of GLP-1, however, interactions with residues residing at the base of the pocket were more transient for exendin-4 (75-80% of the MD frames) than for GLP-1 in the MD simulations (97% of frames for Y152 1 .47 and 100% for R190 2 .60 ) (Supplemental Table 3)
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