Structure-functional analysis of peptide p3 identical to γ370-383, binding sites with integrin αiibβ3 γc-domain of fibrinogen

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Abstract

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 languageEnglish (US)
Pages (from-to)99-105
Number of pages7
JournalUkrain'skyi Biokhimichnyi Zhurnal
Volume75
Issue number6
StatePublished - 2003
Externally publishedYes

Keywords

  • Adhesive reaction
  • Fibrinogen
  • Peptides
  • Platelet intergin

ASJC Scopus subject areas

  • Biochemistry

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