Nature Immunology
6, 810 - 818 (2005)
Published online: 10 July 2005; | doi:10.1038/ni1224
Structure and function of a potent agonist for the semi-invariant natural killer T cell receptorDirk M Zajonc1, Carlos Cantu III2, Jochen Mattner3, Dapeng Zhou3, Paul B Savage4, Albert Bendelac3, Ian A Wilson1, 5
& Luc Teyton21
Department of Molecular Biology and The Scripps Research Institute, La Jolla, California 92037, USA
2
Department of Immunology and The Scripps Research Institute, La Jolla, California 92037, USA
3
Committee on Immunology, University of Chicago, Chicago, Illinois 60637, USA. 4
Brigham Young University, C100 Benson Science Building, Provo, Utah 84602-5700, USA. 5
Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Correspondence should be addressed to Ian A Wilson wilson@scripps.edu or Luc Teyton lteyton@scripps.edu Natural killer T cells express a conserved, semi-invariant   T cell receptor that has specificity for self glycosphingolipids and microbial cell wall -glycuronosylceramide antigens presented by CD1d molecules. Here we report the crystal structure of CD1d in complex with a short-chain synthetic variant of -galactosylceramide at a resolution of 2.2 Å. This structure elucidates the basis for the high specificity of these microbial ligands and explains the restriction of the -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.
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