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 journalArticle

22 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)2371-2383
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number4
DOIs
StatePublished - Jan 24 2014

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Propellers
Fibrin
Integrins
Binding Sites
Clot Retraction
Cell adhesion
Platelets
Cell Adhesion
Thrombosis
Blood Platelets
Mutation

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

The interaction of integrin αiIb β3 with fibrin occurs through multiple binding sites in the α IIb β-propeller domain. / Podolnikova, Nataly; Yakovlev, Sergiy; Yakubenko, Valentin P.; Wang, Xu; Gorkun, Oleg V.; Ugarova, Tatiana.

In: Journal of Biological Chemistry, Vol. 289, No. 4, 24.01.2014, p. 2371-2383.

Research output: Contribution to journalArticle

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AU - Wang, Xu

AU - Gorkun, Oleg V.

AU - Ugarova, Tatiana

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