[HTML][HTML] RGD-containing peptides inhibit fibrinogen binding to platelet αIIbβ3 by inducing an allosteric change in the amino-terminal portion of αIIb
RB Basani, G D'Andrea, N Mitra, G Vilaire… - Journal of Biological …, 2001 - ASBMB
To determine the molecular basis for the insensitivity of rat α IIb β 3 to inhibition by RGD-
containing peptides, hybrids of human and rat α IIb β 3 and chimeras of α IIb β 3 in which α
IIb was composed of portions of human and rat α IIb were expressed in Chinese hamster
ovary cells and B lymphocytes, and the ability of the tetrapeptide RGDS to inhibit fibrinogen
binding to the various forms of α IIb β 3 was measured. These measurements indicated that
sequences regulating the sensitivity of α IIb β 3 to RGDS are located in the seven amino …
containing peptides, hybrids of human and rat α IIb β 3 and chimeras of α IIb β 3 in which α
IIb was composed of portions of human and rat α IIb were expressed in Chinese hamster
ovary cells and B lymphocytes, and the ability of the tetrapeptide RGDS to inhibit fibrinogen
binding to the various forms of α IIb β 3 was measured. These measurements indicated that
sequences regulating the sensitivity of α IIb β 3 to RGDS are located in the seven amino …