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In the MD studies, weaker interactions of oxyntomodulin with residues deep in the cavity, particularly R190 2.60 , were coupled with a loss of stable interactions along the entire face of the TM2 helix and weaker interactions with ECL2, all of which interact with the same face of the helical GLP-1 peptide (Fig

The rationale is to prevent potential receptor desensitization, though clinical evidence for this is limited

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Our data elucidates important mechanism underlying the effects of exendin-4 on adiponectin level both in vitro and in vivo , and shed light on new treatments of diabetes based on exendin-4/GLP-1R functions