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3tn0

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

Structural highlights

3tn0 is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Ligands:	,
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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jayawardena-Wolf J, Benlagha K, Chiu YH, Mehr R, Bendelac A. CD1d endosomal trafficking is independently regulated by an intrinsic CD1d-encoded tyrosine motif and by the invariant chain. Immunity. 2001 Dec;15(6):897-908. PMID:11754812
↑ Zajonc DM, Maricic I, Wu D, Halder R, Roy K, Wong CH, Kumar V, Wilson IA. Structural basis for CD1d presentation of a sulfatide derived from myelin and its implications for autoimmunity. J Exp Med. 2005 Dec 5;202(11):1517-26. Epub 2005 Nov 28. PMID:16314439 doi:10.1084/jem.20051625
↑ Zajonc DM, Cantu C 3rd, Mattner J, Zhou D, Savage PB, Bendelac A, Wilson IA, Teyton L. Structure and function of a potent agonist for the semi-invariant natural killer T cell receptor. Nat Immunol. 2005 Aug;6(8):810-8. Epub 2005 Jul 10. PMID:16007091 doi:10.1038/ni1224
↑ 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. NKT TCR recognition of CD1d-alpha-C-galactosylceramide. J Immunol. 2011 Nov 1;187(9):4705-13. Epub 2011 Sep 30. PMID:21964029 doi:10.4049/jimmunol.1100794