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. 2010 Jul 20;285(40):30951–30958. doi: 10.1074/jbc.M110.102814

FIGURE 1.

FIGURE 1.

Top, two views of the superposition of the three-dimensional models of the N-terminal domain of glucagon receptor constructed using the GIPR and GLP-1R crystal structures. The models built with GIPR and GLP-1R are represented by a purple and green ribbon, respectively. The three disulfide bridges, Asp63, Lys98, and Arg116 are depicted as sticks and colored according to the following color scheme (cyan, carbon; red, oxygen; blue, nitrogen; yellow, sulfur). A salt bridge is formed between Asp63 and Arg116. Similar interactions are observed in the respective x-ray structure templates. Bottom, multiple sequence alignment of the human N-terminal domains of the glucagon, GIP, and GLP-1 receptors used to generate the three-dimensional models of the glucagon receptor. Sequence identity is highlighted in gray.