Fig. 2: The inactive conformation of GLP-1R.
From: Full-length human GLP-1 receptor structure without orthosteric ligands
a Comparison of ECD orientation between the peptide-free GLP-1R–Fab7F38 structure (blue), the active-like peptide 5-bound GLP-1R structure (yellow; PDB: 5NX2), and the active GLP-1-bound GLP-1R–Gs complex structure (orange; PDB: 5VAI). Peptide 5 is shown as sticks with red carbons, GLP-1 is shown in cyan. b Superimposition of the TMDs between the GLP-1R–Fab7F38 (blue) and active GLP-1-bound GLP-1R–Gs complex (orange) structures. Significant changes are highlighted with dashed arrows. The reoriented residue (W214) in ECL1 is shown as sticks, landmark residues (A57ECD, Q211ECL1, T378ECL3) for distance measurements are shown as spheres (Cα).
