Figure 6
Figure 6. Binding of the integrin αIIbβ3 headpiece to the VWF D4-CK fragment. (A) Overall shape of the open αIIbβ3 headpiece (PDB code 2VDR and 3FCS), including the β-propeller and thigh domains in αIIb and PSI, hybrid, βI, and I-EGF1 domains in β3 subunit. Arrow shows the position of the RGD-binding site. (B) Superdex 200 gel filtration of VWF D4-CK, αIIbβ3 headpiece, and their complex in 5mM MnCl2, 0.5mM CaCl2, and 0.1M NaCl and in 20mM buffer of either Bis-Tris, pH 6.2, or HEPES, pH 7.4. (C) EM image of the complex of D4-CK with the αIIbβ3 headpiece at pH 6.2. (D) EM image of the complex of A3-CK with the αIIbβ3 headpiece at pH 6.2. (E) Representative class averages of complex of D4-CK with the αIIbβ3 headpiece. A schematic of integrin binding to VWF is shown to the right. Scale bars represent 50 nm in images and 10 nm in class averages.

Binding of the integrin αIIbβ3 headpiece to the VWF D4-CK fragment. (A) Overall shape of the open αIIbβ3 headpiece (PDB code 2VDR and 3FCS), including the β-propeller and thigh domains in αIIb and PSI, hybrid, βI, and I-EGF1 domains in β3 subunit. Arrow shows the position of the RGD-binding site. (B) Superdex 200 gel filtration of VWF D4-CK, αIIbβ3 headpiece, and their complex in 5mM MnCl2, 0.5mM CaCl2, and 0.1M NaCl and in 20mM buffer of either Bis-Tris, pH 6.2, or HEPES, pH 7.4. (C) EM image of the complex of D4-CK with the αIIbβ3 headpiece at pH 6.2. (D) EM image of the complex of A3-CK with the αIIbβ3 headpiece at pH 6.2. (E) Representative class averages of complex of D4-CK with the αIIbβ3 headpiece. A schematic of integrin binding to VWF is shown to the right. Scale bars represent 50 nm in images and 10 nm in class averages.

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