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. 2015 Oct 9;112(43):13318–13323. doi: 10.1073/pnas.1517862112

Fig. 2.

Fig. 2.

The crystal structure of RLGL-WE14 binding to IAg7. (A) Overview of the crystal structure of the α1/β1 portion of IAg7 in complex with RLGL-WE14 peptide solved at a resolution of 2.4 Å. IAg7 α1 (cyan) and β1 (magenta) are shown as ribbon structures. The RLGL-WE14 peptide is represented as a wireframe with CPK coloring (carbon white, oxygen red, nitrogen blue). The electron density (2Fo − Fc, peptide omit, contoured at 1σ) is shown around the peptide. (B) The solvent accessible surface of the IAg7 complex with RLGL-WE14 (p1 to p9) is shown: IAg7 α1 (cyan), IAg7 β1 (magenta), peptide backbone (white), side chains of anchors p1, p4, p6, and p9 (blue) and p2, p5, p7, and p8 (red). (C) Interactions between amino acids in the p1 pocket and the p1R of RLGL-WE14. (D) Same for p4L. (E) Same for p6S. (F) Same for p9D. (C–F) Wireframe representations O (red), N (blue), S (yellow), C-αIAg7 (cyan), C-βIAg7 (magenta), C-RLGL-WE14 (white), and H-bonds/salt bridges (green).