3u0p
Crystal structure of human CD1d-lysophosphatidylcholine
Structural highlights
FunctionCD1D_HUMAN Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.[1] Publication Abstract from PubMedInvariant Natural Killer T (iNKT) cells use highly restricted alphabeta 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 alpha1 helix resulting in an open A' pocket. Binding of the iNKT TCR requires a 7-A 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 CDR3alpha loop, whereas the remaining CDR loops are shifted, due in part to amino-acid differences in the CDR3beta and Jbeta 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. Lysophospholipid presentation by CD1d and recognition by a human Natural Killer T-cell receptor.,Lopez-Sagaseta J, Sibener LV, Kung JE, Gumperz J, Adams EJ EMBO J. 2012 Mar 6;31(8):2047-59. doi: 10.1038/emboj.2012.54. PMID:22395072[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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