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根据凝血酶原(Prothrombin)环饼结构域-1(PTK-1)2.8晶体X光衍射结构,用残基置换和构型建造(Modeling)预测了纤溶酶原环饼结构域-1(PGK-1),组织型纤溶酶原激活因子环饼结构域-2(PAK-2)和尿激酶原环饼结构域(UKK)的三维结构。预测的三维结构显示PGK-1具有典型的配体结合部位,PAK-2在结构上不具有和配体结合的典型正电荷中心,但邻近的69位精氨酸残基能和配体的羧基生成离子对。UKK在结构上不能形成和配体结合的正负电荷中心,这可能是尿激酶对纤维蛋白低亲和性的主要原因。
According to the X-ray diffraction structure of Prothrombin ring cataract domain-1 (PTK-1) 2.8, the substitution of plasmids and the modeling of plasminogen prcn-1 -1), the three-dimensional structure of PAK-2 and UKK. The predicted three-dimensional structure shows that PGK-1 has a typical ligand binding site, and PAK-2 does not have a structurally positive typical charge center for ligand binding, but the adjacent 69-position arginine residue can bind to the carboxyl Generate ion pairs. UKK is structurally unable to form a positive and negative charge center that binds to the ligand, which may be the main reason for the low affinity of urokinase for fibrin.