Common evolutionary origin of the fibrin‐binding structures of fibronectin and tissue‐type plasminogen activator

FEBS Letters

Patthy, László¹  Bányai, László¹  Váradi, András¹ 

[1] Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, XI. Karolina ut 29, 1113 Budapest, Hungary

关键词: Tissue-type plasminogen activator;    Fibronectin;    Protein evolution;    Fibrin-binding domain;    t-PA;    tissue-type plasminogen activator;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(83)81157-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Comparison of the primary structures of high-M _r urokinase 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.

【 授权许可】

Unknown