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Crystal Structure of Mouse CD1d Bound to the Self Ligand Phosphatidylcholine: A Molecular Basis for NKT Cell Activation^1,2

Barbara Giabbai^*, Stèphane Sidobre, M. D. Max Crispin, Yovan Sanchez-Ruìz, Angela Bachi, Mitchell Kronenberg, Ian A. Wilson and Massimo Degano^3,*

^* Biocrystallography Unit and Mass Spectrometry Unit, DIBIT San Raffaele Scientific Institute, Milan, Italy; Division of Developmental Immunology, La Jolla Institute for Allergy and Immunology, La Jolla, CA 92121; and Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037

NKT cells are immunoregulatory lymphocytes whose activation is triggered by the recognition of lipid Ags in the context of the CD1d molecules by the TCR. In this study we present the crystal structure to 2.8 Å of mouse CD1d bound to phosphatidylcholine. The interactions between the ligand acyl chains and the CD1d molecule define the structural and chemical requirements for the binding of lipid Ags to CD1d. The orientation of the polar headgroup toward the C terminus of the 1 helix provides a rationale for the structural basis for the observed V chain bias in invariant NKT cells. The contribution of the ligand to the protein surface suggests a likely mode of recognition of lipid Ags by the NKT cell TCR.

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