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

doi:10.1074/jbc.M113.518126

The interaction of integrin α_iIb 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 journal › Article › peer-review

37 Scopus citations

Abstract

Background: During thrombus formation, platelet integrin α_IIb 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 α_IIb β₃ has multiple binding sites for fibrin. Significance: Uncovered recognition specificity of α_IIb β₃ for fibrin may be used to select inhibitors of this interaction.

Original language	English (US)
Pages (from-to)	2371-2383
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	289
Issue number	4
DOIs	https://doi.org/10.1074/jbc.M113.518126
State	Published - Jan 24 2014

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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The interaction of integrin α_iIb 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 journal › Article › peer-review

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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.",

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AU - Podolnikova, Nataly

AU - Yakovlev, Sergiy

AU - Yakubenko, Valentin P.

AU - Wang, Xu

AU - Gorkun, Oleg V.

AU - Ugarova, Tatiana

PY - 2014/1/24

Y1 - 2014/1/24

N2 - 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.

AB - 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.

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

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