1Z5L
Structure of a highly potent short-chain galactosyl ceramide agonist bound to CD1D
Summary for 1Z5L
Entry DOI | 10.2210/pdb1z5l/pdb |
Related | 1CD1 |
Descriptor | T-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 Keywords | ig fold, mhc fold, immune system |
Biological source | Mus musculus (house mouse) More |
Total number of polymer chains | 4 |
Total formula weight | 91763.03 |
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 citation | Zajonc, 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: 16007091DOI: 10.1038/ni1224 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
