4EI6
Structure of XV19 Valpha1-Vbeta16 Type-II Natural Killer T cell receptor
Summary for 4EI6
Entry DOI | 10.2210/pdb4ei6/pdb |
Related | 4EI5 |
Descriptor | Valpha1 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 Keywords | natural killer t cell receptor, immune system |
Biological source | Mus musculus, Homo sapiens (mouse, human) More |
Total number of polymer chains | 4 |
Total formula weight | 102580.27 |
Authors | Patel, O.,Rossjohn, J. (deposition date: 2012-04-04, release date: 2012-07-25, Last modification date: 2024-11-20) |
Primary citation | Patel, 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: 22820603DOI: 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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