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Three-Dimensional Structural Aspects of Protein-Polysaccharide Interactions

Journal

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 15, Issue 3, Pages 3768-3783

Publisher

MDPI AG
DOI: 10.3390/ijms15033768

Keywords

polysaccharide; lectin; 3D structure; polylactosamine; galectin; carbohydrate binding module; -glucan; polysialic acid; antibody; affinity; hyaluronan; CD44

Funding

  1. Grants-in-Aid for Scientific Research [25460054] Funding Source: KAKEN

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Linear polysaccharides are typically composed of repeating mono- or disaccharide units and are ubiquitous among living organisms. Polysaccharide diversity arises from chain-length variation, branching, and additional modifications. Structural diversity is associated with various physiological functions, which are often regulated by cognate polysaccharide-binding proteins. Proteins that interact with linear polysaccharides have been identified or developed, such as galectins and polysaccharide-specific antibodies, respectively. Currently, data is accumulating on the three-dimensional structure of polysaccharide-binding proteins. These proteins are classified into two types: exo-type and endo-type. The former group specifically interacts with the terminal units of polysaccharides, whereas the latter with internal units. In this review, we describe the structural aspects of exo-type and endo-type protein-polysaccharide interactions. Further, we discuss the structural basis for affinity and specificity enhancement in the face of inherently weak binding interactions.

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