Heparan sulfate-protein binding specificity

• Published in: Biochemistry (Moscow) Vol. 78; no. 7; pp. 726 - 735
• Main Authors: Nugent, M. A., Zaia, J., Spencer, J. L.
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01.07.2013; Springer; Springer Nature B.V
• Subjects: Animals; Antithrombin III - chemistry; Antithrombin III - metabolism; Biochemistry; Bioinformatics; Biomedical and Life Sciences; Biomedicine; Bioorganic Chemistry; Fibroblast Growth Factors - chemistry; Fibroblast Growth Factors - metabolism; Glycoproteins; Growth factors; Health aspects; Heparan sulfate; Heparitin Sulfate - chemistry; Heparitin Sulfate - metabolism; Humans; Leukocyte Elastase - antagonists & inhibitors; Leukocyte Elastase - metabolism; Life Sciences; Microbiology; Physiological aspects; Polysaccharides; Protein Binding; Protein folding; Proteins - chemistry; Proteins - metabolism; Review; Saccharides; Sulfates; United States; United States > US; heparin; glycosaminoglycans; proteoglycans; heparan sulfate; protein binding; bioinformatics

Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably t...