Structure and binding kinetics of three different human CD1d–α-galactosylceramide–specific T cell receptors
Open Access
- 6 March 2006
- journal article
- Published by Rockefeller University Press in The Journal of Experimental Medicine
- Vol. 203 (3) , 699-710
- https://doi.org/10.1084/jem.20052369
Abstract
Invariant human TCR Vα24-Jα18+/Vβ11+ NKT cells (iNKT) are restricted by CD1d–α-glycosylceramides. We analyzed crystal structures and binding characteristics for an iNKT TCR plus two CD1d–α-GalCer–specific Vβ11+ TCRs that use different TCR Vα 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–α-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)3α, CDR3β, and CDR1β interact with ligands presented by CD1d, whereas CDR2β binds to the CD1d α1 helix. This docking provides an explanation for the dominant usage of Vβ11 and Vβ8.2 chains by human and mouse iNKT cells, respectively, for recognition of CD1d–α-GalCer.Keywords
This publication has 55 references indexed in Scilit:
- Structural and kinetic basis for heightened immunogenicity of T cell vaccinesThe Journal of Experimental Medicine, 2005
- Molecular Mechanism of Lipopeptide Presentation by CD1aImmunity, 2005
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- ARP⧸wARP and Automatic Interpretation of Protein Electron Density MapsPublished by Elsevier ,2003
- Use of TLS parameters to model anisotropic displacements in macromolecular refinementActa Crystallographica Section D-Biological Crystallography, 2001
- Canonical structures for the hypervariable regions of T cell αβ receptorsJournal of Molecular Biology, 2000
- Polyalanine Reconstruction from Cα Positions Using the ProgramCALPHACan Aid Initial Phasing of Data by Molecular Replacement ProceduresActa Crystallographica Section D-Biological Crystallography, 1997
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 ÅJournal of Molecular Biology, 1979