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2PO6

Crystal structure of CD1d-lipid-antigen complexed with Beta-2-Microglobulin, NKT15 Alpha-Chain and NKT15 Beta-Chain

Summary for 2PO6
Entry DOI10.2210/pdb2po6/pdb
DescriptorT-cell surface glycoprotein CD1d, Beta-2-microglobulin, NKT15 alpha-chain, ... (8 entities in total)
Functional Keywordscd1d-lipid antigen nkt15 complex, lipid binding protein-immune system complex, lipid binding protein/immune system
Biological sourceHomo sapiens (human)
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Total number of polymer chains8
Total formula weight191075.65
Authors
Borg, N.A. (deposition date: 2007-04-25, release date: 2007-07-03, Last modification date: 2024-12-25)
Primary citationBorg, N.A.,Wun, K.S.,Kjer-Nielsen, L.,Wilce, M.C.,Pellicci, D.G.,Koh, R.,Besra, G.S.,Bharadwaj, M.,Godfrey, D.I.,McCluskey, J.,Rossjohn, J.
CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor.
Nature, 448:44-49, 2007
Cited by
PubMed Abstract: The CD1 family is a large cluster of non-polymorphic, major histocompatibility complex (MHC) class-I-like molecules that bind distinct lipid-based antigens that are recognized by T cells. The most studied group of T cells that interact with lipid antigens are natural killer T (NKT) cells, which characteristically express a semi-invariant T-cell receptor (NKT TCR) that specifically recognizes the CD1 family member, CD1d. NKT-cell-mediated recognition of the CD1d-antigen complex has been implicated in microbial immunity, tumour immunity, autoimmunity and allergy. Here we describe the structure of a human NKT TCR in complex with CD1d bound to the potent NKT-cell agonist alpha-galactosylceramide, the archetypal CD1d-restricted glycolipid. In contrast to T-cell receptor-peptide-antigen-MHC complexes, the NKT TCR docked parallel to, and at the extreme end of the CD1d-binding cleft, which enables a lock-and-key type interaction with the lipid antigen. The structure provides a basis for the interaction between the highly conserved NKT TCR alpha-chain and the CD1d-antigen complex that is typified in innate immunity, and also indicates how variability of the NKT TCR beta-chain can impact on recognition of other CD1d-antigen complexes. These findings provide direct insight into how a T-cell receptor recognizes a lipid-antigen-presenting molecule of the immune system.
PubMed: 17581592
DOI: 10.1038/nature05907
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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