2Z35
Crystal structure of immune receptor
Summary for 2Z35
Entry DOI | 10.2210/pdb2z35/pdb |
Descriptor | T-cell receptor alpha-chain, T-cell receptor beta-chain (3 entities in total) |
Functional Keywords | immune receptor, immune system |
Biological source | Mus musculus (house mouse) More |
Total number of polymer chains | 2 |
Total formula weight | 24475.75 |
Authors | Feng, D.,Bond, C.J.,Ely, L.K.,Garcia, K.C. (deposition date: 2007-06-01, release date: 2007-10-09, Last modification date: 2024-10-30) |
Primary citation | Feng, D.,Bond, C.J.,Ely, L.K.,Maynard, J.,Garcia, K.C. Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon' Nat.Immunol., 8:975-983, 2007 Cited by PubMed 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 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'. PubMed: 17694060DOI: 10.1038/ni1502 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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