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  • Title: Multivalent ligand binding by serum mannose-binding protein.
    Author: Lee RT, Ichikawa Y, Kawasaki T, Drickamer K, Lee YC.
    Journal: Arch Biochem Biophys; 1992 Nov 15; 299(1):129-36. PubMed ID: 1280063.
    Abstract:
    The serum-type mannose-binding protein (MBP) is a defense molecule that has carbohydrate-dependent bactericidal effects. It shares with mammalian and chicken hepatic lectins similarity in the primary structure of the carbohydrate-recognition domain, as well as the ligand-binding mode: a high affinity (KD approximately nM) is generated by clustering of approximately 30 terminal target sugar residues on a macromolecule, such as bovine serum albumin, although the individual monosaccharides have low affinity (KD 0.1-1 mM). On the other hand, MBP does not manifest any significant affinity enhancement toward small, di- and trivalent ligands, in contrast to the hepatic lectins whose affinity toward divalent ligands of comparable structures increased from 100- to 1000-fold. Such differences may be explained on the basis of different subunit organization between the hepatic lectins and MBP.
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