The interaction of integrin αiIb β3 with fibrin occurs through multiple binding sites in the α IIb β-propeller domain

Abstract

Background: During thrombus formation, platelet integrin αIIb β3 binds fibrin; however, the mechanism of this interaction is unclear. Results: Mutations of discontinuous negatively charged and aromatic residues in the α IIb β-propeller domain impair fibrin clot retraction and cell adhesion. Conclusion: Integrin αIIb β3 has multiple binding sites for fibrin. Significance: Uncovered recognition specificity of αIIb β3 for fibrin may be used to select inhibitors of this interaction. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.