3tn0 | pdb_00003tn0

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

spinqualitylabelsall models 3tn0, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tn0 is a 4 chain structure with sequence from Human and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG, QUX Related: 3qux Gene: Cd1d1, Cd1.1 (LK3 transgenic mice), B2m, RP23-34E24.5-001, mCG_11606 (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CD1D1_MOUSE] Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Publication Abstract from PubMed NKT cells respond to a variety of CD1d-restricted glycolipid Ags that are structurally related to the prototypic Ag alpha-galactosylceramide (alpha-GalCer). A modified analog of alpha-GalCer with a carbon-based glycosidic linkage (alpha-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 alpha-C-GalCer, and related C-glycoside ligands, is weaker than that of alpha-GalCer. Furthermore, the Vbeta8.2 and Vbeta7 NKT TCR affinity for CD1d-alpha-C-GalCer, and some related analogs, is approximately 10-fold lower than that for the NKT TCR-CD1d-alpha-GalCer interaction. Nevertheless, the crystal structure of the Vbeta8.2 NKT TCR-CD1d-alpha-C-GalCer complex is similar to that of the corresponding NKT TCR-CD1d-alpha-GalCer complex, although subtle differences at the interface provide a basis for understanding the lower affinity of the NKT TCR-CD1d-alpha-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. NKT TCR recognition of CD1d-alpha-C-galactosylceramide.,Patel O, Cameron G, Pellicci DG, Liu Z, Byun HS, Beddoe T, McCluskey J, Franck RW, Castano AR, Harrak Y, Llebaria A, Bittman R, Porcelli SA, Godfrey DI, Rossjohn J J Immunol. 2011 Nov 1;187(9):4705-13. Epub 2011 Sep 30. PMID:21964029 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures CD1

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