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) |
|---|---|
| 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 |
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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 journal › Article
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TY - JOUR
T1 - The interaction of integrin αiIb β3 with fibrin occurs through multiple binding sites in the α IIb β-propeller domain
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.
UR - http://www.scopus.com/inward/record.url?scp=84893118880&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84893118880&partnerID=8YFLogxK
U2 - 10.1074/jbc.M113.518126
DO - 10.1074/jbc.M113.518126
M3 - Article
VL - 289
SP - 2371
EP - 2383
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 4
ER -