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Nat Immunol. 2005 Aug;6(8):754-6.
Structure and function of a potent agonist for the semi-invariant natural killer T cell receptor.
Department of Molecular Biology and The Scripps Research Institute, La Jolla, California 92037, USA.
Natural killer T cells express a conserved, semi-invariant alphabeta T cell receptor that has specificity for self glycosphingolipids and microbial cell wall alpha-glycuronosylceramide antigens presented by CD1d molecules. Here we report the crystal structure of CD1d in complex with a short-chain synthetic variant of alpha-galactosylceramide at a resolution of 2.2 A. This structure elucidates the basis for the high specificity of these microbial ligands and explains the restriction of the alpha-linkage as a unique pathogen-specific pattern-recognition motif. Comparison of the binding of altered lipid ligands to CD1d and T cell receptors suggested that the differential T helper type 1-like and T helper type 2-like properties of natural killer T cells may originate largely from differences in their 'loading' in different cell types and hence in their tissue distribution in vivo.
PMID: 16007091 [PubMed - indexed for MEDLINE]
PMCID: PMC2045075
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Cited by 17 PubMed Central articles
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[Proc Natl Acad Sci U S A. 2009]
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Determination of cellular lipids bound to human CD1d molecules.
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[Mol Immunol. 2009]
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