Sandbox Reserved 1660: Difference between revisions

Additionally, there are two <scene name='86/868193/Oligosaccharides/1'>oligosaccharides</scene> bound to the alpha chain via [https://en.wikipedia.org/wiki/N-linked_glycosylation N-glycosylations] and three types of small molecules bound to that protein<ref name="Structure"/>. CD1d molecules are structurally similar to [[Major Histocompatibility Complex Class I]], but present lipid antigens as opposed to peptides and the cleft where the ligand can bind its protein is different between MHC molecules and CD1d molecules. Indeed, the hydrophobic cleft of CD1d has a narrow opening.The recognition between the protein and its ligand occurs at a specific spot which creates an appropriate environment for the interaction to happen. This <scene name='86/868193/Site/1'>site</scene> is located at the A and F pockets in the region of the alpha helices<ref name="site">Schiefner, A.; Fujio, M.; Wu, D.; Wong, C.-H.; Wilson, I. A. Structural Evaluation of Potent NKT-Cell Agonists: Implications for Design of Novel Stimulatory Ligands. J Mol Biol 2009, 394 (1), 71–82. https://doi.org/10.1016/j.jmb.2009.08.061</ref>.

</p>

== Impact of ligand-binding ==

CD1 molecules can also be used as NKT cell markers. Indeed, a CD1 molecule can be engineered to become [https://en.wikipedia.org/wiki/Fluorescence fluorescent] by binding a fluorescent-potent molecule to it. When the engineered complex interacts with a NKT cell, the fluorescent signal is emitted and therefore the NKT cells can be spotted<ref>Benlagha, K., Weiss, A., Beavis, A., Teyton, L., & Bendelac, A. (2000). In vivo identification of glycolipid antigen-specific T cells using fluorescent CD1d tetramers. The Journal of experimental medicine, 191(11), 1895–1903. https://doi.org/10.1084/jem.191.11.1895</ref>.  

</p>

==See Also==