The interactions between platelet integrin αIIbβ 3 and fibrinogen (Fg) mediate a range of adhesive reactions, which are necessary for platelet aggregation and fibrin clot retraction. The binding site for α,IIbβ3 resides in the γC domain of Fg. In our previous work we have identified a novel binding site in the γC domain, γ370-383 (P3), for integrin α IIbα3 and have demonstrated that the P3 sequence together with the C-terminal γC sequence 408AGDV411 accounts for the full binding of αIIbβ3. In our present study, in order to define the amino acid residues in P3 involved in the interaction with αIIbβ3, we have used SPOT-synthesis analyses. Libraries consisting of peptides covering P3 were created and probed with radiolabeled αIIbβ3. Screening of the libraries showed that several positively charged residues may be critical for interaction of P3 with integrin αIIbβ 3.
|Original language||English (US)|
|Number of pages||7|
|Journal||Ukrain'skyi Biokhimichnyi Zhurnal|
|State||Published - 2003|
- Adhesive reaction
- Platelet intergin
ASJC Scopus subject areas