Fig. 3: Crystal structure of αVβ3/Hr10 complex. | Nature Communications

Fig. 3: Crystal structure of αVβ3/Hr10 complex.

From: Structure-guided design of pure orthosteric inhibitors of αIIbβ3 that prevent thrombosis but preserve hemostasis

Fig. 3

a Ribbon diagram of the crystal structure of αVβ3-bound Hr10 (same view as Fig. 1a) showing 2fo–fc map at 1.0 σ (blue mesh) of the ligand-binding region. Relevant portions of Hr10 (light green), αV propeller (light blue), and the βA domain of β3 subunit (rose color) are shown. Side chains of amino acids (single letter code) are shown as sticks in the respective colors. The Mn2+ ions at LIMBS, MIDAS, and ADMIDAS are in grey, cyan, and magenta spheres, respectively. Oxygen, nitrogen, and sulfur atoms are colored as in Fig. 1a. Water molecules are not shown. Hr10’s W1496 forms a π–π interaction with βA-Y122, and Hr10-Har1493 forms a bidentate salt bridge with αV-D218. b Ribbon diagrams of the crystal structures of Hr10/αVβ3 (light green) and eptifibatide/αIIbβ3 (light purple, 2vdn.pdb) superposed on the βA domain of each. View, domain, side chain, and metal ion colors are as in a. Note the removal of the predicted clash of Hr10 with D2-A3 loop of αIIb and predicted formation of Hr10-Har1493/αIIb-D224 salt bridge.

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