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

Nataly Podolnikova, Sergiy Yakovlev, Valentin P. Yakubenko, Xu Wang, Oleg V. Gorkun, Tatiana Ugarova

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


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 languageEnglish (US)
Pages (from-to)2371-2383
Number of pages13
JournalJournal of Biological Chemistry
Issue number4
StatePublished - Jan 24 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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