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PDBsum entry 5efi
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Immune system
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PDB id
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5efi
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References listed in PDB file
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Key reference
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Title
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Structure of an α-Helical peptide and lipopeptide bound to the nonclassical major histocompatibility complex (mhc) class i molecule cd1d.
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Authors
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E.Girardi,
J.Wang,
D.M.Zajonc.
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Ref.
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J Biol Chem, 2016,
291,
10677-10683.
[DOI no: ]
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PubMed id
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Abstract
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Mouse CD1d is a nonclassical MHC molecule able to present lipids and glycolipids
to a specialized subset of T cells known as natural killer T cells. The antigens
presented by CD1d have been shown to cover a broad range of chemical structures
and to follow precise rules determining the potency of the antigen in the
context of T cell activation. Together with lipids, initial reports suggested
that CD1d can also bind and present hydrophobic peptides with (F/W)XX(I/L/M)XXW.
However, the exact location of peptide binding and the molecular basis for the
required motif are currently unknown. Here we present the crystal structure of
the first peptide identified to bind CD1d, p99, and show that it binds in the
antigen-binding groove of CD1d in a manner compatible with its presentation to T
cell receptors. Interestingly, the peptide adopts an α-helical conformation,
which orients the motif residues toward its deep binding groove, therefore
explaining the molecular requirements for peptide binding. Moreover, we
demonstrate that a lipopeptide version of the same peptide is able to bind CD1d
in a similar conformation, identifying another class of molecules binding this
antigen-presenting molecule.
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