Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TZV

Crystal structure of an iNKT TCR in complex with CD1d-lysophosphatidylcholine

Summary for 3TZV
Entry DOI10.2210/pdb3tzv/pdb
Related3TYF 3U0P
DescriptorInvariant Natural Killer T Cell Receptor chain A, Invariant Natural Killer T Cell Receptor chain B, Antigen-presenting glycoprotein CD1d, ... (10 entities in total)
Functional Keywordsimmunoglobulin-like, mhc class i-like, antigen recognition, cd1d, cell surface, immune system
Biological sourceHomo sapiens (human)
More
Total number of polymer chains6
Total formula weight149943.37
Authors
Lopez-Sagaseta, J.,Adams, E.J. (deposition date: 2011-09-27, release date: 2012-04-25, Last modification date: 2024-11-20)
Primary citationLopez-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: 22395072
DOI: 10.1038/emboj.2012.54
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.056 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon