title: Glycosylation assists binding of HIV protein gp120 to human CD4 receptor.
abstract: The role of glycosylation of proteins on its binding affinity is not well understood. Even a monosaccharide (magenta) placed at a glycosylation site can significantly enhance binding of peptides to their receptor. If glycosylated, an HIV protein binds stronger and faster to its primary receptors on human cells.
authors.affiliation: Organic Chemistry, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.
authors.forename: Dennis
authors.initials: D
authors.lastname: Wilhelm
authors.forename: Henning N
authors.initials: HN
authors.lastname: Behnken
authors.forename: Bernd
authors.initials: B
authors.lastname: Meyer
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D015704:CD4 Antigens / Q000737:chemistry* / Q000378:metabolism*; D006031:Glycosylation; D015699:HIV Envelope Protein gp120 / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data
chemical_list: D015704:CD4 Antigens; D015699:HIV Envelope Protein gp120