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2.12: Glycoproteins

  • Page ID
    4237
  • Glycoproteins have carbohydrate attached to them — a process called glycosylation. The attachment is a covalent linkage to:

    • the hydroxyl (-OH) group of the R group of serine or threonine - called "O-linked" in both cases or to
    • the amino group (-NH2) in the R group of asparagine - called "N-linked"

    The carbohydrate consists of short, usually branched, chains of

    • plain sugars (e.g., glucose, galactose)
    • amino sugars (sugars with an amino group, e.g., N-acetylglucosamine), and
    • acidic sugars (sugars with a carboxyl group, e.g., sialic acid)

    Sugars are very hydrophilic thanks to their many -OH groups. Their presence

    • makes glycoproteins far more hydrophilic than they would be otherwise and
    • are often essential for the proper folding of the protein into its tertiary structure

    Most of the proteins exposed to the watery surroundings at the surface of cells are glycoproteins.

    Glycophorin spans a lipid bilayer, with carbohydrate chains attached to its extracellular region.A chain of labeled amino-acid circles runs from the N-terminal end outside the cell, through the lipid bilayer, to the C-terminal end inside. Residue numbers mark positions along the chain. The key identifies blue O-linked carbohydrate symbols attached to orange Ser or Thr residues, and green N-linked carbohydrate attached to a dark blue Asn residue. These carbohydrate attachments occur on the outside portion; the membrane-spanning and inside portions have none shown. The bilayer is drawn as two rows of heads with tails facing inward.This image shows the primary structure of glycophorin A, a glycoprotein that spans the plasma membrane ("Lipid bilayer") of human red blood cells. Each RBC has some 500,000 copies of the molecule embedded in its plasma membrane.

    • Fifteen carbohydrate chains are "O-linked" to serine (Ser) and threonine (Thr) residues
    • One carbohydrate chain is "N-linked" to the asparagine (Asn) at position 26

    Two polymorphic versions of glycophorin A, which differ only at residues 1 and 5, occur in humans. These give rise to the MN blood groups

    • The M allele encodes Ser at position 1 (Ser-1) and Gly at position 5 (Gly-5)
    • The N allele encodes Leu-1 and Glu-5

    Genotype to Phenotype

    Individuals who inherit two N alleles (are homozygous) have blood group N.

    • Individuals who are homozygous for the M allele have blood group M.
    • Heterozygous individuals produce both proteins and have blood group MN.

    Glycophorin A is the most important attachment site by which the parasite Plasmodium falciparum invades human red blood cells.


    This page titled 2.12: Glycoproteins is shared under a CC BY 3.0 (creativecommons.org) license and was authored, remixed, and/or curated by John W. Kimball (biology-pages.info) via source content (biology-pages.info) that was edited to the style and standards of the LibreTexts platform.


    2.12: Glycoproteins is shared under a CC BY 3.0 license and was authored, remixed, and/or curated by LibreTexts.

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