Next Article in Journal
Inhibition of Acetylcholinesterase Modulates NMDA Receptor Antagonist Mediated Alterations in the Developing Brain
Next Article in Special Issue
Towards Controlling the Glycoform: A Model Framework Linking Extracellular Metabolites to Antibody Glycosylation
Previous Article in Journal
Killing Me Softly—Future Challenges in Apoptosis Research
Previous Article in Special Issue
Gram-Negative Flagella Glycosylation
Int. J. Mol. Sci. 2014, 15(3), 3768-3783; doi:10.3390/ijms15033768
Review

Three-Dimensional Structural Aspects of Protein–Polysaccharide Interactions

 and
*
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
* Author to whom correspondence should be addressed.
Received: 26 December 2013 / Revised: 17 February 2014 / Accepted: 21 February 2014 / Published: 3 March 2014
(This article belongs to the Special Issue Glycosylation and Glycoproteins)
View Full-Text   |   Download PDF [2540 KB, uploaded 19 June 2014]   |  

Abstract

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.
Keywords: polysaccharide; lectin; 3D structure; polylactosamine; galectin; carbohydrate binding module; β-glucan; polysialic acid; antibody; affinity; hyaluronan; CD44 polysaccharide; lectin; 3D structure; polylactosamine; galectin; carbohydrate binding module; β-glucan; polysialic acid; antibody; affinity; hyaluronan; CD44
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
SciFeed

Share & Cite This Article

Further Mendeley | CiteULike
Export to BibTeX |
EndNote |
RIS
MDPI and ACS Style

Nagae, M.; Yamaguchi, Y. Three-Dimensional Structural Aspects of Protein–Polysaccharide Interactions. Int. J. Mol. Sci. 2014, 15, 3768-3783.

View more citation formats

Related Articles

Article Metrics

For more information on the journal, click here

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert