Three-Dimensional Structural Aspects of Protein–Polysaccharide Interactions

International Journal of Molecular Sciences

Masamichi Nagae¹ 

[1]Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan

[2] E-Mail

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

DOI  :  10.3390/ijms15033768

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland