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The study also focused only on semaglutide, and the findings cannot be immediately generalized to other GLP-1 drugs

GLP-1 Binding The EM structure of the GLP-1 apo receptor (i.e., receptor in the absence of any ligand), shows that the N-terminal domain adopts a closed or inactive conformation, where a cap-like structure blocks access to the peptide binding ( PDB ID 6ln2, Wu et al., 2020, Figure 4a)

[17] [14] This remains a theoretical consideration under investigation

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