Heteroaromatic Moieties in the Sphingosine Backbone of α-Galactosylceramides for Noncovalent Interactions with CD1d
Related Experiment Video
Updated: Apr 28, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Yongju Kim1, Jonghoon Kim1, Keunhee Oh2
1Department of Chemistry, Seoul National University , Seoul, Korea.
Abstract:
A series of α-GalCer analogues containing heterocyclic and aromatic moieties in the sphingosine backbone were synthesized to improve the selectivity in the Th1/Th2 cytokine profile via noncovalent interaction with three aromatic residues at the binding pocket of CD1d. In vitro and in vivo biological evaluations revealed the treatment of α-GalCer analogue (6) induced the selective stimulation of natural killer T cells to facilitate the secretion of Th2 cytokines.
Related Concept Videos
Immunoglobulin-like Cell Adhesion Molecules
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Lipids as Anchors
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
Membrane Lipids
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
Proteoglycans
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Membrane Carbohydrates
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...

