The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine

Tetranectin, a homotrimeric protein belonging to the family of C-type lectins and structurally highly related to corresponding regions of the mannose-binding proteins, is known specifically to bind the plasminogen kringle 4 protein domain, an interaction sensitive to lysine. Surface plasmon resonanc...

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Veröffentlicht in:The Journal of biological chemistry 1998-10, Vol.273 (44), p.29241-29246
Hauptverfasser: Graversen, Jonas Heilskov, Lorentsen, Rikke Høegh, Jacobsen, Christian, Moestrup, Søren K., Sigurskjold, Bent W., Thøgersen, Hans Christian, Etzerodt, Michael
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Sprache:eng
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Zusammenfassung:Tetranectin, a homotrimeric protein belonging to the family of C-type lectins and structurally highly related to corresponding regions of the mannose-binding proteins, is known specifically to bind the plasminogen kringle 4 protein domain, an interaction sensitive to lysine. Surface plasmon resonance and isothermal calorimetry binding analyses using single-residue and deletion mutant tetranectin derivatives produced in Escherichia coli showed that the kringle 4 binding site resides in the carbohydrate recognition domain and includes residues of the putative carbohydrate binding site. Furthermore, the binding analysis revealed that the interaction is sensitive to calcium in addition to lysine.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.44.29241