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. 2013 Jun 24;201(7):1053–1068. doi: 10.1083/jcb.201212037

Figure 2.

Figure 2.

The RGD-binding pocket. (A–J) The αIIbβ3 headpiece states are native closed (A; Zhu et al., 2012); the states indicated in Table 1 (B–I), and native open (J; Springer et al., 2008) are shown. Residues that contribute to the RGD-binding pocket are shown both as sticks and transparent surfaces in light blue (αIIb) and wheat (β3). Metal ions are shown as yellow (SyMBS and ADMIDAS) or cyan (MIDAS) spheres. Waters are smaller red spheres. GRGDSP peptides are shown in stick with green carbons. Oxygens and nitrogens are red and blue, respectively. Composite omit simulated-annealing electron density is in black mesh contoured at 3 σ for SyMBS and MIDAS metal ions, 1 σ (except 0.5 σ in E and F) for ADMIDAS metal ion, and 0.5 σ for waters and GRGDSP peptide. Hydrogen bonds and metal ion coordination bonds are dashed.