Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8319397 | Current Opinion in Structural Biology | 2018 | 8 Pages |
Abstract
Heparan sulfate interacts with a variety of proteins at the cell surface. These proteins are primarily attracted to the high negative charge distribution brought by sulfate, sulfamate, and carboxylate functionalities along the sugar chain. Apart from electrostatic interactions, hydrogen bonding and even hydrophobic interactions contribute to the complex formation. While additional sulfate/sulfamate groups are often tolerated as long as the main structural requirements are met, occasionally, certain extra sulfate groups may be detrimental to the binding affinity. Here, we show these binding characteristics using the binding of fibroblast growth factors and heparin-binding hemagglutinin to synthetic heparan sulfate oligosaccharides as examples. Insights into the binding characteristics of these proteins may benefit future therapeutic interventions.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Medel Manuel L Zulueta, Chia-Lin Chyan, Shang-Cheng Hung,