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

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Abstract

Comparison of the primary structures of high-Mr 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.

Original languageEnglish
Pages (from-to)37-41
Number of pages5
JournalFEBS letters
Volume163
Issue number1
DOIs
Publication statusPublished - Oct 31 1983

Keywords

  • Fibrin-binding domain
  • Fibronectin
  • Protein evolution
  • Tissue-type plasminogen activator

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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