Fig. 2: Interactions between SST β-turn residues and SSTR2 transmembrane residues. | Cell Discovery

Fig. 2: Interactions between SST β-turn residues and SSTR2 transmembrane residues.

From: Structural insights into the activation of somatostatin receptor 2 by cyclic SST analogues

Fig. 2: Interactions between SST β-turn residues and SSTR2 transmembrane residues.

a Ca2+ response of SSTR2 with SST14, octreotide, and lanreotide. Data are presented as means ± SEM of three independent experiments conducted in triplicate. b Local density maps of SST14, octreotide and lanreotide. The conserved key binding amino acids are highlighted. ce Superposition of the ligand-binding pockets of SST14- or octreotide- or lanreotide-bound SSTR2 receptor. fh Ca2+ accumulation analysis of wild-type (WT) SSTR2 and mutants with SST14 (f) or octreotide (g) or lanreotide (h). Site mutations around the ligand-binding pocket disrupted the receptor–ligand interactions, resulting in SSTR2 malfunction in the Ca2+ accumulation assay. Data are presented as means ± SEM of three independent experiments conducted in triplicate.

Back to article page