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2Z31

Crystal structure of immune receptor complex

Summary for 2Z31
Entry DOI10.2210/pdb2z31/pdb
Related1K2D
DescriptorT-cell receptor alpha-chain, T-cell receptor beta-chain, H-2 class II histocompatibility antigen, A-U alpha chain, ... (5 entities in total)
Functional Keywordsimmune system, complex
Biological sourceMus musculus (house mouse)
More
Cellular locationMembrane; Single-pass type I membrane protein (Potential): P14438 P06344
Total number of polymer chains5
Total formula weight68633.99
Authors
Feng, D.,Bond, C.J.,Ely, L.K.,Garcia, K.C. (deposition date: 2007-05-30, release date: 2007-10-09, Last modification date: 2024-10-23)
Primary citationFeng, 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: 17694060
DOI: 10.1038/ni1502
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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