3HE6
Crystal structure of mouse CD1d-alpha-galactosylceramide with mouse Valpha14-Vbeta8.2 NKT TCR
Summary for 3HE6
| Entry DOI | 10.2210/pdb3he6/pdb |
| Related | 3HE7 |
| Descriptor | Antigen-presenting glycoprotein CD1d1, Beta-2-microglobulin, Valpha14(mouse variable domain, human constant domain), ... (8 entities in total) |
| Functional Keywords | mouse cd1d, mouse nkt t-cell receptors, cell membrane, disulfide bond, endosome, glycoprotein, immune response, immunoglobulin domain, innate immunity, lysosome, membrane, transmembrane, mhc i, immune system |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 97993.62 |
| Authors | Patel, O.,Rossjohn, J. (deposition date: 2009-05-07, release date: 2009-07-28, Last modification date: 2024-10-30) |
| Primary citation | Pellicci, D.G.,Patel, O.,Kjer-Nielsen, L.,Pang, S.S.,Sullivan, L.C.,Kyparissoudis, K.,Brooks, A.G.,Reid, H.H.,Gras, S.,Lucet, I.S.,Koh, R.,Smyth, M.J.,Mallevaey, T.,Matsuda, J.L.,Gapin, L.,McCluskey, J.,Godfrey, D.I.,Rossjohn, J. Differential recognition of CD1d-alpha-galactosyl ceramide by the V beta 8.2 and V beta 7 semi-invariant NKT T cell receptors Immunity, 31:47-59, 2009 Cited by PubMed Abstract: The semi-invariant natural killer T cell receptor (NKT TCR) recognizes CD1d-lipid antigens. Although the TCR alpha chain is typically invariant, the beta chain expression is more diverse, where three V beta chains are commonly expressed in mice. We report the structures of V alpha 14-V beta 8.2 and V alpha 14-V beta 7 NKT TCRs in complex with CD1d-alpha-galactosylceramide (alpha-GalCer) and the 2.5 A structure of the human NKT TCR-CD1d-alpha-GalCer complex. Both V beta 8.2 and V beta 7 NKT TCRs and the human NKT TCR ligated CD1d-alpha-GalCer in a similar manner, highlighting the evolutionarily conserved interaction. However, differences within the V beta domains of the V beta 8.2 and V beta 7 NKT TCR-CD1d complexes resulted in altered TCR beta-CD1d-mediated contacts and modulated recognition mediated by the invariant alpha chain. Mutagenesis studies revealed the differing contributions of V beta 8.2 and V beta 7 residues within the CDR2 beta loop in mediating contacts with CD1d. Collectively we provide a structural basis for the differential NKT TCR V beta usage in NKT cells. PubMed: 19592275DOI: 10.1016/j.immuni.2009.04.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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