Lesson 4.2. Glycoconjugates
Lesson 4.2. Glycoconjugates
Lesson 4.2. Glycoconjugates
2: Glycoconjugates
Lesson Summary
This lesson will discuss the different association of carbohydrates with other non-carbohydrate
molecules. This will also discuss the importance and functions of glycoconjugates.
Learning Outcomes
At the end of this lesson, the student should be able to:
Motivation Question
What are other molecules attached to carbohydrates?
Discussion
Glycoconjugates
Glycolipids
Glycolipids are glycoconjugates of carbohydrates and lipids and is common among membrane
lipids.
The lipids are generally hydrophobic (water fearing) and the oligosaccharides are hydrophilic.
Glycolipids generally serve as a surface recognition site.
Figure 55. Structure of glycolipids
Glycoproteins
Glycoproteins are glycoconjugate of proteins and carbohydrates and has a wide variable
composition (microheterogeneity). It also has a large array of functions such as for structure,
transport, enzymes, receptors, etc. The carbohydrate chains are often short (oligosaccharides),
though not all, and may be branched. The carbohydrate moiety is synthesized by enzymatic
reaction and covalently linked to polypeptide (protein component).
Glycoproteins serve several biological importance aside from its structural functions. It also acts
as surface recognition, specifically the carbohydrate component, such as the syndecan.
Syndecan are human membrane core protein with heparan sulfate carbohydrate units.
Figure 56. Glycoproteins embedded in the plasma membrane
This glycoprotein plays a very important role in the prevention of blood clot. The carbohydrate
unit in this glycoprotein has a sulfated monosaccharide chain (NS domain) which is serves as
binding site for the antithrombin (AT) molecule.
Figure 58. The binding of AT to the S domain lading to the conformational change for factor Xa to attach
In the presence of the sulfated monosaccharide chain in the glycoprotein, the protein
antithrombin will attached causing it to have a conformational change in its structure. This
conformational change of the antithrombin will allow its interaction with Factor Xa, a blood
clotting factor. Without the conformational change of AT, due to its binding to the sulfated
carbohydrate moiety in syndecan, factor Xa cannot bind to AT thus uncontrolled bleeding may
occur.
On the other hand, if thrombin and antithrombin molecules are present, it will bind to two
adjacent NS domains in the heparan sulfate bringing the two proteins in closer proximity which
will lead to its interaction. The attached thrombin to the AT will inhibit the interaction of factor Xa.
In this case blood clotting will be inhibited.