COMMON EVOLUTIONARY ORIGIN OF THE FIBRIN-BINDING STRUCTURES OF FIBRONECTIN AND TISSUE-TYPE PLASMINOGEN-ACTIVATOR
COMMON EVOLUTIONARY ORIGIN OF THE FIBRIN-BINDING STRUCTURES OF FIBRONECTIN AND TISSUE-TYPE PLASMINOGEN-ACTIVATOR
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DOI：
10.1016/0014-5793(83)81157-0
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发表时间：
1983-01-01
期刊：
影响因子：
3.5
通讯作者：
PATTHY, L
中科院分区：
文献类型：
--
作者：
BANYAI, L;VARADI, A;PATTHY, L
高尿激酶和组织型纤溶酶原激活物的初级结构比较表明，除了组织型激活物含有43个残基氨基末端区域外，两种蛋白在结构上具有高度的同源性，这在尿激酶中没有对应的氨基酸末端区域。我们发现该片段与负责纤维连接蛋白的纤维蛋白亲和力的手指结构域同源。发现纤溶酶原激活物氨基末端区域的有限蛋白水解导致该酶的纤维蛋白亲和力丧失。这表明纤维连接蛋白和组织型纤溶酶原激活物的手指结构域具有相似的功能，并且这两种蛋白的手指结构域是从一个共同的祖先纤维蛋白结合结构域进化而来的。
Comparison of the primary structures of high‐Mrurokinase and tissue‐type plasminogen activator reveals a high degree of structural homology between the two proteins, except that tissue activator contains a 43 residue long amino‐terminal region, which has no counterpart in urokinase. We show that this segment is homologous with the finger‐domains responsible for the fibrin‐affinity of fibronectin. Limited proteolysis of the amino‐terminal region of plasminogen activator was found to lead to a loss of the fibrin‐affinity of the enzyme. It is suggested that the finger‐domains of fibronectin and tissue‐types plasminogen activator have similar functions and that the finger‐domains of the two proteins evolved from a common ancestral fibrin‐binding domain.