3TZV
Crystal structure of an iNKT TCR in complex with CD1d-lysophosphatidylcholine
Summary for 3TZV
Entry DOI | 10.2210/pdb3tzv/pdb |
Related | 3TYF 3U0P |
Descriptor | Invariant Natural Killer T Cell Receptor chain A, Invariant Natural Killer T Cell Receptor chain B, Antigen-presenting glycoprotein CD1d, ... (10 entities in total) |
Functional Keywords | immunoglobulin-like, mhc class i-like, antigen recognition, cd1d, cell surface, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 6 |
Total formula weight | 149943.37 |
Authors | Lopez-Sagaseta, J.,Adams, E.J. (deposition date: 2011-09-27, release date: 2012-04-25, Last modification date: 2024-11-20) |
Primary citation | Lopez-Sagaseta, J.,Sibener, L.V.,Kung, J.E.,Gumperz, J.,Adams, E.J. Lysophospholipid presentation by CD1d and recognition by a human Natural Killer T-cell receptor. Embo J., 31:2047-2059, 2012 Cited by PubMed Abstract: Invariant Natural Killer T (iNKT) cells use highly restricted αβ T cell receptors (TCRs) to probe the repertoire of lipids presented by CD1d molecules. Here, we describe our studies of lysophosphatidylcholine (LPC) presentation by human CD1d and its recognition by a native, LPC-specific iNKT TCR. Human CD1d presenting LPC adopts an altered conformation from that of CD1d presenting glycolipid antigens, with a shifted α1 helix resulting in an open A' pocket. Binding of the iNKT TCR requires a 7-Å displacement of the LPC headgroup but stabilizes the CD1d-LPC complex in a closed conformation. The iNKT TCR CDR loop footprint on CD1d-LPC is anchored by the conserved positioning of the CDR3α loop, whereas the remaining CDR loops are shifted, due in part to amino-acid differences in the CDR3β and Jβ segment used by this iNKT TCR. These findings provide insight into how lysophospholipids are presented by human CD1d molecules and how this complex is recognized by some, but not all, human iNKT cells. PubMed: 22395072DOI: 10.1038/emboj.2012.54 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.056 Å) |
Structure validation
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