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

Bányai, László, Váradi, András, Patthy, László·1983·FEBS Letters

Abstract

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.

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Metadata

Authors
Bányai, L., Váradi, A., & Patthy, L.
Venue
FEBS Letters
Publisher
Wiley
Published
1983-10-31
Volume
163
Issue
1
Pages
37-41
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2040551353
Cited by
237
References
0
FWCI
12.51
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Common evolutionary origin of the fibrin‐binding structures of fibronectin and tissue‐type plasminogen activator. https://app.cochat.ai/papers/10.1016/0014-5793(83)81157-0
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Bányai, L., Váradi, A., & Patthy, L. (1983). Common evolutionary origin of the fibrin‐binding structures of fibronectin and tissue‐type plasminogen activator. FEBS Letters. https://doi.org/10.1016/0014-5793(83)81157-0

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