3C6L

Crystal structure of mouse MHC class II I-Ab/3K peptide complexed with mouse TCR 2W20

Summary for 3C6L

• Entry DOI: 10.2210/pdb3c6l/pdb
• Related: 1LNU 3C5Z 3C60
• Descriptor: TCR 2W20 alpha chain, TCR 2W20 beta chain, H-2 class II histocompatibility antigen, A-B alpha chain, ... (5 entities in total)
• Functional Keywords: tcr-pmhc complex, glycoprotein, immune response, membrane, mhc ii, transmembrane, sugar binding protein-immune system complex, sugar binding protein/immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane ; Single-pass type I membrane protein : P14434
• Total number of polymer chains: 8
• Total formula weight: 186083.04

Authors

Dai, S. (deposition date: 2008-02-04, release date: 2008-04-29, Last modification date: 2024-10-30)

Primary citation

Dai, S.,Huseby, E.S.,Rubtsova, K.,Scott-Browne, J.,Crawford, F.,Macdonald, W.A.,Marrack, P.,Kappler, J.W.
Crossreactive T Cells spotlight the germline rules for alphabeta T cell-receptor interactions with MHC molecules.
Immunity, 28:324-334, 2008

PubMed Abstract: To test whether highly crossreactive alphabeta T cell receptors (TCRs) produced during limited negative selection best illustrate evolutionarily conserved interactions between TCR and major histocompatibility complex (MHC) molecules, we solved the structures of three TCRs bound to the same MHC II peptide (IAb-3K). The TCRs had similar affinities for IAb-3K but varied from noncrossreactive to extremely crossreactive with other peptides and MHCs. Crossreactivity correlated with a shrinking, increasingly hydrophobic TCR-ligand interface, involving fewer TCR amino acids. A few CDR1 and CDR2 amino acids dominated the most crossreactive TCR interface with MHC, including Vbeta8 48Y and 54E and Valpha4 29Y, arranged to impose the familiar diagonal orientation of TCR on MHC. These interactions contribute to MHC binding by other TCRs using related V regions, but not usually so dominantly. These data show that crossreactive TCRs can spotlight the evolutionarily conserved features of TCR-MHC interactions and that these interactions impose the diagonal docking of TCRs on MHC.

PubMed: 18308592
DOI: 10.1016/j.immuni.2008.01.008

Experimental method

X-RAY DIFFRACTION (3.4 Å)