ArticleThe Journal of biological chemistry2016
Structure of an α-Helical Peptide and Lipopeptide Bound to the Nonclassical Major Histocompatibility Complex (MHC) Class I Molecule CD1d.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Crystal structures of lysophospholipid-bound MHC class I molecules.The Journal of biological chemistry · 2020Article
- Distinct CD1d docking strategies exhibited by diverse Type II NKT cell receptors.Nature communications · 2019Article
- Structural basis of NKT cell inhibition using the T-cell receptor-blocking anti-CD1d antibody 1B1.The Journal of biological chemistry · 2019Article
- CD1d-Restricted Type II NKT Cells Reactive With Endogenous Hydrophobic Peptides.Frontiers in immunology · 2018Review
- Mechanisms and Consequences of Antigen Presentation by CD1.Trends in immunology · 2016Review
- The CD1 family: serving lipid antigens to T cells since the Mesozoic era.Immunogenetics · 2016Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
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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Registered trials
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