2PXY

Crystal structures of immune receptor complexes

Summary for 2PXY

• Entry DOI: 10.2210/pdb2pxy/pdb
• Related: 1K2D
• Descriptor: T cell receptor alpha chain, T cell receptor beta chain, H-2 class II histocompatibility antigen, A-U alpha chain, ... (6 entities in total)
• Functional Keywords: complex, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein (Potential): P14438 P06344
• Total number of polymer chains: 5
• Total formula weight: 69387.72

Authors

Feng, D.,Bond, C.J.,Ely, L.K.,Garcia, K.C. (deposition date: 2007-05-14, 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

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

Experimental method

X-RAY DIFFRACTION (2.23 Å)