Structural evidence for a germline-encoded T cell receptor–major histocompatibility complex interaction 'codon'
- 12 August 2007
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Immunology
- Vol. 8 (9), 975-983
- https://doi.org/10.1038/ni1502
Abstract
All complexes of T cell receptors (TCRs) bound to peptide–major histocompatibility complex (pMHC) molecules assume a stereotyped binding 'polarity', despite wide variations in TCR-pMHC docking angles. However, existing TCR-pMHC crystal structures have failed to show broadly conserved pairwise interaction motifs. Here we determined the crystal structures of two TCRs encoded by the variable β-chain 8.2 (Vβ8.2), each bound to the MHC class II molecule I-Au, and did energetic mapping of Vα and Vβ contacts with I-Au. Together with two previously solved structures of Vβ8.2-containing TCR-MHC complexes, we found four TCR–I-A complexes with structurally superimposable interactions between the Vβ loops and the I-A α-helix. This examination of a narrow 'slice' of the TCR-MHC repertoire demonstrates what is probably one of many germline-derived TCR-MHC interaction 'codons'.Keywords
This publication has 47 references indexed in Scilit:
- How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?The EMBO Journal, 2007
- How the T Cell Repertoire Becomes Peptide and MHC SpecificCell, 2005
- Molecular Recognition by a Binary CodeJournal of Molecular Biology, 2005
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Identification of a Crucial Energetic Footprint on the α1 Helix of Human Histocompatibility Leukocyte Antigen (Hla)-A2 That Provides Functional Interactions for Recognition by Tax Peptide/Hla-A2–Specific T Cell ReceptorsThe Journal of Experimental Medicine, 2001
- Role of 2c T Cell Receptor Residues in the Binding of Self–And Allo–Major Histocompatibility ComplexesThe Journal of Experimental Medicine, 2000
- Canonical structures for the hypervariable regions of T cell αβ receptorsJournal of Molecular Biology, 2000
- Dual conformations of a T cell receptor Vα homodimer: implications for variability in VαVβ domain associationJournal of Molecular Biology, 1997
- Structure, function and properties of antibody binding sitesJournal of Molecular Biology, 1991
- Canonical structures for the hypervariable regions of immunoglobulinsJournal of Molecular Biology, 1987