2CDF
Structure and binding kinetics of three different human CD1d-alpha- Galactosylceramide-specific T cell receptors (TCR 5E)
Summary for 2CDF
| Entry DOI | 10.2210/pdb2cdf/pdb |
| Related | 1AO7 1B88 1BD2 1BWM 1CD1 1D9K 1FO0 1FYT 1G6R 1H5B 1HXM 1J8H 1KB5 1KGC 1KJ2 1KTK 1L0Y 1LP9 1MI5 1MWA 1NAM 1NFD 1QRN 1QSE 1QSF 1TCR 1TVD 1YMM 1YPZ 1Z5L 1ZHN 1ZT4 2AKR 2AXH 2AXJ 2BNQ 2BNR 2BNU 2CDE 2CDG 2CKB |
| Descriptor | TCR 5E (3 entities in total) |
| Functional Keywords | cell receptor, cd1d, alpha-galactosylceramide, non-canonical tcr, tcr, t cell receptor, mhc class i, natural killer t cell, tcr 5e |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 2 |
| Total formula weight | 48832.09 |
| Authors | Gadola, S.D.,Koch, M.,Marles-Wright, J.,Lissin, N.M.,Sheperd, D.,Matulis, G.,Harlos, K.,Villiger, P.M.,Stuart, D.I.,Jakobsen, B.K.,Cerundolo, V.,Jones, E.Y. (deposition date: 2006-01-23, release date: 2006-03-07, Last modification date: 2024-10-23) |
| Primary citation | Gadola, S.D.,Koch, M.,Marles-Wright, J.,Lissin, N.M.,Sheperd, D.,Matulis, G.,Harlos, K.,Villiger, P.M.,Stuart, D.I.,Jakobsen, B.K.,Cerundolo, V.,Jones, E.Y. Structrue and Binding Kinetics of Three Different Human Cd1D-Alpha-Galactosylceramide-Specific T Cell Receptors J.Exp.Med., 203:699-, 2006 Cited by PubMed Abstract: Invariant human TCR Valpha24-Jalpha18+/Vbeta11+ NKT cells (iNKT) are restricted by CD1d-alpha-glycosylceramides. We analyzed crystal structures and binding characteristics for an iNKT TCR plus two CD1d-alpha-GalCer-specific Vbeta11+ TCRs that use different TCR Valpha chains. The results were similar to those previously reported for MHC-peptide-specific TCRs, illustrating the versatility of the TCR platform. Docking TCR and CD1d-alpha-GalCer structures provided plausible insights into their interaction. The model supports a diagonal orientation of TCR on CD1d and suggests that complementarity determining region (CDR)3alpha, CDR3beta, and CDR1beta interact with ligands presented by CD1d, whereas CDR2beta binds to the CD1d alpha1 helix. This docking provides an explanation for the dominant usage of Vbeta11 and Vbeta8.2 chains by human and mouse iNKT cells, respectively, for recognition of CD1d-alpha-GalCer. PubMed: 16520393DOI: 10.1084/JEM.20052369 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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