Glycoprotein

A protein with one or more carbohydrate chains covalently attached. These chains can influence its folding, stability, transport, and recognition.

Protein: A molecule made of one or more chains of amino acids folded into a functional structure. The protein supplies the backbone to which carbohydrate chains are attached.
N-linked glycosylation: The attachment of a sugar chain to the nitrogen atom of an asparagine side chain in a protein. It is a major route for adding carbohydrate chains to proteins entering the secretory pathway.
Monoclonal antibody: An antibody produced by a single cell lineage and designed to bind a particular molecular target. Therapeutic antibodies are glycoproteins whose attached sugars can alter their activity.
Proteoglycan: A protein bearing one or more long glycosaminoglycan chains, often found in extracellular matrices. Its long, repeating sugar chains distinguish it from most glycoproteins.
Lectin: A protein that binds specific carbohydrate structures without catalyzing their modification. Lectins recognize glycoprotein sugars and mediate binding or cellular sorting.
Carbohydrate: A molecule composed mainly of carbon, hydrogen, and oxygen, including sugars and their polymers. Carbohydrate chains form the attached portion of a glycoprotein.
O-linked glycosylation: The attachment of sugars to oxygen atoms in serine, threonine, or other protein side chains. It adds carbohydrate at sites distinct from the asparagine sites used in N-linked glycosylation.
Erythropoietin: A hormone produced mainly by the kidneys that stimulates red blood cell production. Its carbohydrate chains help determine stability and persistence in circulation.
Glycolipid: A lipid with one or more carbohydrate groups covalently attached. It carries sugars on a lipid backbone rather than a protein backbone.
Calnexin: An endoplasmic-reticulum chaperone that binds particular glucose-bearing N-linked glycans on proteins. It uses glycan structure to help monitor glycoprotein folding.

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