Shimomura T, Fujimura K
Department of Internal Medicine, Hiroshima University.
Rinsho Ketsueki. 1994 Mar;35(3):224-9.
Platelet glycoprotein (GP) IIb-IIIa (alpha IIb beta 3) binds fibrinogen with high affinity. To identify structure responsible for the alpha IIb beta 3 specific fibrinogen binding, chimeric receptors between alpha IIb and alpha v were constructed, expressed on heterologous cells, and their function was analyzed. Chimeric receptors with mutations in calcium binding sequences showed similar ligand specificity as wild type receptor. However, those with replacements in amino-terminal regions revealed substitutions of the epitopes for specific receptor-blocking antibodies, indicating importance of this amino-terminal region for alpha IIb beta 3 specific ligand recognition.
血小板糖蛋白（GP）IIb-IIIa（αIIbβ3）以高亲和力结合纤维蛋白原。为了确定负责αIIbβ3特异性纤维蛋白原结合的结构，构建了αIIb和αv之间的嵌合受体，在异源细胞上表达，并分析其功能。钙结合序列发生突变的嵌合受体表现出与野生型受体相似的配体特异性。然而，那些在氨基末端区域被替换的受体显示出特异性受体阻断抗体表位的替换，表明该氨基末端区域对于αIIbβ3特异性配体识别的重要性。
