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J. Biol. Chem., Vol. 275, Issue 48, 37390-37396, December 1, 2000

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Mutational Analysis of Affinity and Selectivity of Kringle-Tetranectin Interaction
GRAFTING NOVEL KRINGLE AFFINITY ONTO THE TETRANECTIN LECTIN SCAFFOLD^*

Jonas Heilskov Graversen, Christian Jacobsen^§, Bent W. Sigurskjold^¶, Rikke Høegh Lorentsen, Søren K. Moestrup^§, Hans Christian Thøgersen, and Michael Etzerodt

From the  Laboratory of Gene Expression, Department of Molecular and Structural Biology and the ^§ Department of Medical Biochemistry, University of Aarhus, DK-8000 Aarhus C, Denmark, and ^¶ August Krogh Institute, University of Copenhagen, Denmark, DK-2100 Copenhagen Ø, Denmark

C-type lectin-like domains are found in many proteins, where they mediate binding to a wide diversity of compounds, including carbohydrates, lipids, and proteins. The binding of a C-type lectin-like domain to a ligand is often influenced by calcium. Recently, we have identified a site in the C-type lectin-like domain of tetranectin, involving Lys-148, Glu-150, and Asp-165, which mediates calcium-sensitive binding to plasminogen kringle 4. Here, we investigate the effect of conservative substitutions of these and a neighboring amino acid residue. Substitution of Thr-149 in tetranectin with a tyrosine residue considerably increases the affinity for plasminogen kringle 4, and, in addition, confers affinity for plasminogen kringle 2. As shown by isothermal titration calorimetry analysis, this new interaction is stronger than the binding of wild-type tetranectin to plasminogen kringle 4. This study provides further insight into molecular determinants of importance for binding selectivity and affinity of C-type lectin kringle interactions.

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