Fig. 3: Comparisons of the GLP-1R conformations and binding pockets stabilised by GLP-1, exendin-4, oxyntomodulin and exendin-P5.
From: Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation
a Superimposition of the receptor from the GLP-1R:Gs complex structures bound with GLP-1 (6X1816—receptor-blue, peptide-orange), oxyntomodulin (receptor-dark pink, peptide-pale yellow), exendin-4 (receptor-pale green, peptide-purple) and exendin-P5 (6B3J13—receptor-pale orange, peptide-cyan). Middle, Overlay of full-length receptors with bound peptides; Left, close up of an extracellular portion of the receptor TMD viewed from the side (top) and looking down on the TMD-binding cavity (bottom); Right, close up of the ECD showing the distinct location of the ECD N-terminal α-helix and the location of the peptide C-terminus in the different structures (top) and the receptor TM domain viewed from the intracellular G protein binding site. b Superimposition of the peptide binding sites within the GLP-1R TMD comparing GLP-1 with oxyntomodulin (left), GLP-1 with exendin-4 (middle) and exendin-4 with exendin-P5 (right). Colouring denotes the different peptide bound receptors as highlighted on the figure panels.
