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Tetranectin, a trimeric plasminogen-binding C-type lectin

T L Holtet1, J H Graversen, I Clemmensen

  • 1Department of Molecular and Structural Biology, University of Aarhus, Denmark.

Protein Science : a Publication of the Protein Society
|July 1, 1997
PubMed
Summary
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Tetranectin, a plasminogen-binding protein, forms a stable homo-trimer in solution. Its N-terminal domain is essential for this subunit trimerization, a key characteristic of collectin family members.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Tetranectin is a plasminogen-binding protein within the C-type lectin family.
  • Collectins, another group of C-type lectins, are known to form homo-trimers.

Purpose of the Study:

  • To characterize the oligomeric state of recombinant and natural tetranectin.
  • To identify the specific domain responsible for tetranectin subunit trimerization.

Main Methods:

  • Expression of tetranectin in E. coli.
  • In vitro refolding and proteolytic processing.
  • Chemical cross-linking analysis and SDS-PAGE.

Main Results:

  • Recombinant and natural tetranectin exist as homo-trimers in solution.

Related Experiment Videos

  • An N-terminal domain, encoded by exons 1 and 2, was identified as necessary and sufficient for trimerization.

    • Conclusions:

    • Tetranectin shares the homo-trimeric structure characteristic of collectins.
    • The N-terminal domain of tetranectin plays a crucial role in mediating subunit assembly.