Figure 6
Figure 6. Conformational change of integrin αIIbβ3 headpiece studied by gel filtration and dynamic light scattering. (A) Gel filtration profile of αIIbβ3 headpiece alone or bound with antagonists. The untagged αIIbβ3 headpiece was mixed with saturating amounts of RUC-1, tirofiban, or eptifibatide and incubated at room temperature for 1 hour before Superdex 200 chromatography in Tris-buffered saline with 1mM Ca2+/Mg2+. The elution volumes are shown in parentheses. (B) Stokes radius measured by gel filtration or dynamic light scattering. (C-D) The structures with surface representation indicate the putative conformational rearrangement after drug binding. The structures were generated by adding the αIIb thigh domain from the complete ectodomain structure to the headpiece crystal structures. The Ca2+ and Mg2+ ions are shown as yellow and silver spheres, respectively. RUC-1 (C) and tirofiban (D) are shown as spheres.

Conformational change of integrin αIIbβ3 headpiece studied by gel filtration and dynamic light scattering. (A) Gel filtration profile of αIIbβ3 headpiece alone or bound with antagonists. The untagged αIIbβ3 headpiece was mixed with saturating amounts of RUC-1, tirofiban, or eptifibatide and incubated at room temperature for 1 hour before Superdex 200 chromatography in Tris-buffered saline with 1mM Ca2+/Mg2+. The elution volumes are shown in parentheses. (B) Stokes radius measured by gel filtration or dynamic light scattering. (C-D) The structures with surface representation indicate the putative conformational rearrangement after drug binding. The structures were generated by adding the αIIb thigh domain from the complete ectodomain structure to the headpiece crystal structures. The Ca2+ and Mg2+ ions are shown as yellow and silver spheres, respectively. RUC-1 (C) and tirofiban (D) are shown as spheres.

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