1ZHN

Crystal Structure of mouse CD1d bound to the self ligand phosphatidylcholine

Summary for 1ZHN

• Entry DOI: 10.2210/pdb1zhn/pdb
• Related: 1CD1 1GZP 1GZQ 1ONQ
• Descriptor: CD1d1 antigen, beta-2-microglobulin, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: mhc fold; antigen binding domain; ig fold, immune system, membrane protein
• Biological source: Mus musculus (house mouse); More
• Cellular location: Secreted: P01887
• Total number of polymer chains: 2
• Total formula weight: 45377.25

Authors

Giabbai, B.,Sidobre, S.,Crispin, M.M.D.,Sanchez Ruiz, Y.,Bachi, A.,Kronenberg, M.,Wilson, I.A.,Degano, M. (deposition date: 2005-04-26, release date: 2005-07-19, Last modification date: 2024-10-30)

Primary citation

Giabbai, B.,Sidobre, S.,Crispin, M.M.D.,Sanchez Ruiz, Y.,Bachi, A.,Kronenberg, M.,Wilson, I.A.,Degano, M.
Crystal structure of mouse CD1d bound to the self ligand phosphatidylcholine: a molecular basis for NKT cell activation
J.Immunol., 175:977-984, 2005

PubMed Abstract: 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 A 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 alpha1 helix provides a rationale for the structural basis for the observed Valpha 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.

PubMed: 16002697

Experimental method

X-RAY DIFFRACTION (2.8 Å)