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. Author manuscript; available in PMC: 2023 Feb 11.
Published in final edited form as: Adv Protein Chem Struct Biol. 2011;84:143–180. doi: 10.1016/B978-0-12-386483-3.00001-X

Fig. 5.

Fig. 5.

Structural insights into Ptprg–Cntn4 interactions. (A) The Ptprg–Cntn4 complex in two view related by a 30° rotation along a vertical axis. Mouse Cntn4 is shown in surface representation according to the color coding introduced in Fig. 4. The CA domain of mouse Ptprg is shown using a ribbontprg diagram and is colored magenta. In the second view, only the binding regions of Ptprg are shown and they consist of two loop regions. (B) The Ptprg-binding site on Cntn4 spans Ig domains 2 and 3. Ig domains 1, 2, 3, and 4 are colored cyan, green, gold, and red, respectively. Amino acids in Cntn4 that are in contact with amino acids in Ptprg are colored magenta. (C) Conservation of amino acids at the interface between Ptprg and Cntn4. Black lines denote van der Waals interactions, whereas red lines indicate potential hydrogen bonds and salt bridges. Amino acids in the green and gold boxes are located in Ig2 and Ig3 of Cntn4, respectively.