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1Z5L

Structure of a highly potent short-chain galactosyl ceramide agonist bound to CD1D

Summary for 1Z5L
Entry DOI10.2210/pdb1z5l/pdb
Related1CD1
DescriptorT-cell surface glycoprotein CD1d antigen, Beta-2-microglobulin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordsig fold, mhc fold, immune system
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains4
Total formula weight91763.03
Authors
Zajonc, D.M.,Cantu, C.,Mattner, J.,Zhou, D.,Savage, P.B.,Bendelac, A.,Wilson, I.A.,Teyton, L. (deposition date: 2005-03-18, release date: 2005-07-19, Last modification date: 2024-10-30)
Primary citationZajonc, D.M.,Cantu, C.,Mattner, J.,Zhou, D.,Savage, P.B.,Bendelac, A.,Wilson, I.A.,Teyton, L.
Structure and function of a potent agonist for the semi-invariant natural killer T cell receptor.
Nat.Immunol., 6:810-818, 2005
Cited by
PubMed Abstract: 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.
PubMed: 16007091
DOI: 10.1038/ni1224
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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