novel non-peptide fibrinogen receptor antagonist, induces conformational changes in glycoprotein lib/lila

نویسندگان

  • Tomoko SATOH
  • William C. KOUNS
  • Yuko YAMASHITA
  • Tsutomu KAMIYAMA
  • Beat STEINERt
چکیده

Arg-Gly-Asp (RGD) is an amino acid sequence in fibrinogen recognized by platelet glycoprotein (GP) lIb/IlIa. Recently, it was found that RGD peptide binding to GPIIb/IIIa leads to conformational changes in the complex that are associated with the acquisition of high-affinity fibrinogen-binding function. In this study, we found that tetrafibricin, a novel non-peptidic GPIIb/IIIa antagonist, induced similar conformational changes in GPIIb/IIIa as did RGD peptides. Tetrafibricin increased the binding of purified inactive GPIIb/IIIa to immobilized pl-80, a

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تاریخ انتشار 2005