Abstract
Glycosaminoglycans (GAGs) constitute a considerable fraction of the glycoconjugates found on cellular membranes and in the extracellular matrix of virtually all mammalian tissues. The essential role of GAG-protein interactions in the regulation of physiological processes has been recognized for decades. However, the underlying molecular basis of these interactions has only emerged since 1990s. The binding specificity of GAGs is encoded in their primary structures, but ultimately depends on how their functional groups are presented to a protein in the three-dimensional space. This review focuses on the application of NMR spectroscopy on the characterization of the GAG-protein interactions. Examples of interpretation of the complex mechanism and characterization of structural motifs involved in the GAG-protein interactions are given. Selected families of GAG-binding proteins investigated using NMR are also described.
Highlights
Glycosaminoglycans (GAGs) are linear acidic heteropolysaccharides that exist in all mammals and are formed by repeating disaccharide units composed of N-acetyl-hexosamine and hexuronic or hexose (Table 1; Vasconcelos and Pomin, 2017)
The results showed that IdoA2S, which replaced glucuronic acid (GlcA), was in a pure 1C4 conformation when bound, and the affinity was tripled, which provided a basis for the application of bovine heparin
It can provide information about the binding affinity constant, on/off chemical exchange rate, binding site and atomic information, but high-precision research is more demanding for technology
Summary
National Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Qingdao, China. Reviewed by: Xiaojun Sun, University of Jinan, China Yasuteru Shigeta, University of Tsukuba, Japan. Glycosaminoglycans (GAGs) constitute a considerable fraction of the glycoconjugates found on cellular membranes and in the extracellular matrix of virtually all mammalian tissues. The essential role of GAG-protein interactions in the regulation of physiological processes has been recognized for decades. The binding specificity of GAGs is encoded in their primary structures, but depends on how their functional groups are presented to a protein in the three-dimensional space. This review focuses on the application of NMR spectroscopy on the characterization of the GAG-protein interactions. Examples of interpretation of the complex mechanism and characterization of structural motifs involved in the GAG-protein interactions are given. Selected families of GAG-binding proteins investigated using NMR are described
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