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.
Original language | English (US) |
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Pages (from-to) | 2371-2383 |
Number of pages | 13 |
Journal | Journal of Biological Chemistry |
Volume | 289 |
Issue number | 4 |
DOIs | |
State | Published - Jan 24 2014 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology