3TN0

Structure of mouse Va14Vb8.2NKT TCR-mouse CD1d-a-C-Galactosylceramide complex

Summary for 3TN0

• Entry DOI: 10.2210/pdb3tn0/pdb
• Related: 3QUX
• Descriptor: Antigen-presenting glycoprotein CD1d1, Beta-2 microglobulin, mouse NKT Valpha14 (MOUSE VARIABLE DOMAIN, HUMAN CONSTANT DOMAIN), ... (7 entities in total)
• Functional Keywords: mouse cd1d, mouse nkt, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 4
• Total formula weight: 97991.65

Authors

Patel, O.,Rossjohn, J. (deposition date: 2011-09-01, release date: 2011-12-14, Last modification date: 2024-10-30)

Primary citation

Patel, O.,Cameron, G.,Pellicci, D.G.,Liu, Z.,Byun, H.S.,Beddoe, T.,McCluskey, J.,Franck, R.W.,Castano, A.R.,Harrak, Y.,Llebaria, A.,Bittman, R.,Porcelli, S.A.,Godfrey, D.I.,Rossjohn, J.
NKT TCR Recognition of CD1d-{alpha}-C-Galactosylceramide.
J.Immunol., 187:4705-4713, 2011

PubMed Abstract: NKT cells respond to a variety of CD1d-restricted glycolipid Ags that are structurally related to the prototypic Ag α-galactosylceramide (α-GalCer). A modified analog of α-GalCer with a carbon-based glycosidic linkage (α-C-GalCer) has generated great interest because of its apparent ability to promote prolonged, Th1-biased immune responses. In this study, we report the activation of spleen NKT cells to α-C-GalCer, and related C-glycoside ligands, is weaker than that of α-GalCer. Furthermore, the Vβ8.2 and Vβ7 NKT TCR affinity for CD1d-α-C-GalCer, and some related analogs, is ∼10-fold lower than that for the NKT TCR-CD1d-α-GalCer interaction. Nevertheless, the crystal structure of the Vβ8.2 NKT TCR-CD1d-α-C-GalCer complex is similar to that of the corresponding NKT TCR-CD1d-α-GalCer complex, although subtle differences at the interface provide a basis for understanding the lower affinity of the NKT TCR-CD1d-α-C-GalCer interaction. Our findings support the concept that for CD1d-restricted NKT cells, altered glycolipid ligands can promote markedly different responses while adopting similar TCR-docking topologies.

PubMed: 21964029
DOI: 10.4049/jimmunol.1100794

Experimental method

X-RAY DIFFRACTION (3.2 Å)