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Publication Abstract from PubMed

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 beta-chain 8.2 (V(beta)8.2), each bound to the MHC class II molecule I-A(u), and did energetic mapping of V(alpha) and V(beta) contacts with I-A(u). Together with two previously solved structures of V(beta)8.2-containing TCR-MHC complexes, we found four TCR-I-A complexes with structurally superimposable interactions between the V(beta) loops and the I-A alpha-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'.

Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'.,Feng D, Bond CJ, Ely LK, Maynard J, Garcia KC Nat Immunol. 2007 Sep;8(9):975-83. Epub 2007 Aug 12. PMID:17694060^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.