Terminal sialic acids on CD44 N-glycans can block hyaluronan binding by forming competing intramolecular contacts with arginine sidechains.

Faller, Christina E; Guvench, Olgun

Faller, Christina E; Guvench, Olgun.

Affiliation

Faller CE; Department of Pharmaceutical Sciences, University of New England College of Pharmacy, ortland, Maine, 04103.

Proteins ; 82(11): 3079-89, 2014 Nov.

Article in En | MEDLINE | ID: mdl-25116630

Subject(s)

Hyaluronan Receptors/chemistry; Hyaluronan Receptors/metabolism; Hyaluronic Acid/metabolism; Polysaccharides/chemistry; Polysaccharides/metabolism; Arginine/metabolism; Asparagine/chemistry; Binding Sites; Carbohydrate Sequence; Glycosylation; Humans; Hydrogen Bonding; Models, Molecular; Molecular Dynamics Simulation; Molecular Sequence Data; Protein Conformation; Sialic Acids/chemistry; Sialic Acids/metabolism

Key words

carbohydrate; charge pairing; extracellular matrix; glycosylation; hydrogen bond; molecular dynamics

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Polysaccharides / Hyaluronan Receptors / Hyaluronic Acid Limits: Humans Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 2014 Document type: Article Country of publication: United States

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