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4EI6

Structure of XV19 Valpha1-Vbeta16 Type-II Natural Killer T cell receptor

Summary for 4EI6
Entry DOI10.2210/pdb4ei6/pdb
Related4EI5
DescriptorValpha1 XV19 Type II Natural Killer T cell receptor (mouse variable domain, human constant domain), Vbeta16 XV19 Type II Natural Killer T cell receptor (mouse variable domain, human constant domain) (3 entities in total)
Functional Keywordsnatural killer t cell receptor, immune system
Biological sourceMus musculus, Homo sapiens (mouse, human)
More
Total number of polymer chains4
Total formula weight102580.27
Authors
Patel, O.,Rossjohn, J. (deposition date: 2012-04-04, release date: 2012-07-25, Last modification date: 2024-11-20)
Primary citationPatel, O.,Pellicci, D.G.,Gras, S.,Sandoval-Romero, M.L.,Uldrich, A.P.,Mallevaey, T.,Clarke, A.J.,Le Nours, J.,Theodossis, A.,Cardell, S.L.,Gapin, L.,Godfrey, D.I.,Rossjohn, J.
Recognition of CD1d-sulfatide mediated by a type II natural killer T cell antigen receptor.
Nat.Immunol., 13:857-863, 2012
Cited by
PubMed Abstract: Natural killer T cells (NKT cells) are divided into type I and type II subsets on the basis of differences in their T cell antigen receptor (TCR) repertoire and CD1d-antigen specificity. Although the mode by which type I NKT cell TCRs recognize CD1d-antigen has been established, how type II NKT cell TCRs engage CD1d-antigen is unknown. Here we provide a basis for how a type II NKT cell TCR, XV19, recognized CD1d-sulfatide. The XV19 TCR bound orthogonally above the A' pocket of CD1d, in contrast to the parallel docking of type I NKT cell TCRs over the F' pocket of CD1d. At the XV19 TCR-CD1d-sulfatide interface, the TCRα and TCRβ chains sat centrally on CD1d, where the malleable CDR3 loops dominated interactions with CD1d-sulfatide. Accordingly, we highlight the diverse mechanisms by which NKT cell TCRs can bind CD1d and account for the distinct antigen specificity of type II NKT cells.
PubMed: 22820603
DOI: 10.1038/ni.2372
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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