Tetranectin, a trimeric plasminogen-binding C-type lectin. |
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Authors: | T. L. Holtet, J. H. Graversen, I. Clemmensen, H. C. Th gersen, M. Etzerodt |
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Affiliation: | T. L. Holtet, J. H. Graversen, I. Clemmensen, H. C. Thøgersen, and M. Etzerodt |
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Abstract: | Tetranectin, a plasminogen-binding protein belonging to the family of C-type lectins, was expressed in E. coli and converted to its native form by in vitro refolding and proteolytic processing. Recombinant tetranectin-as well as natural tetranectin from human plasma-was shown by chemical cross-linking analysis and SDS-PAGE to be a homo-trimer in solution as are other known members of the collectin family of C-type lectins. Biochemical evidence is presented showing that an N-terminal domain encoded within exons 1 and 2 of the tetranectin gene is necessary and sufficient to govern subunit trimerization. |
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Keywords: | C-lectin domain structure refolding trimerization |
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