1D9K

CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA

Summary for 1D9K

• Entry DOI: 10.2210/pdb1d9k/pdb
• Descriptor: T-CELL RECEPTOR D10 (ALPHA CHAIN), T-CELL RECEPTOR D10 (BETA CHAIN), MHC I-AK A CHAIN (ALPHA CHAIN), ... (7 entities in total)
• Functional Keywords: t-cell receptor, mhc class ii, d10, i-ak, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 10
• Total formula weight: 141227.13

Authors

Reinherz, E.L.,Tan, K.,Tang, L.,Kern, P.,Liu, J.-H.,Xiong, Y.,Hussey, R.E.,Smolyar, A.,Hare, B.,Zhang, R.,Joachimiak, A.,Chang, H.-C.,Wagner, G.,Wang, J.-H. (deposition date: 1999-10-28, release date: 1999-12-15, Last modification date: 2024-11-20)

Primary citation

Reinherz, E.L.,Tan, K.,Tang, L.,Kern, P.,Liu, J.,Xiong, Y.,Hussey, R.E.,Smolyar, A.,Hare, B.,Zhang, R.,Joachimiak, A.,Chang, H.C.,Wagner, G.,Wang, J.
The crystal structure of a T cell receptor in complex with peptide and MHC class II.
Science, 286:1913-1921, 1999

PubMed Abstract: The crystal structure of a complex involving the D10 T cell receptor (TCR), 16-residue foreign peptide antigen, and the I-Ak self major histocompatibility complex (MHC) class II molecule is reported at 3.2 angstrom resolution. The D10 TCR is oriented in an orthogonal mode relative to its peptide-MHC (pMHC) ligand, necessitated by the amino-terminal extension of peptide residues projecting from the MHC class II antigen-binding groove as part of a mini beta sheet. Consequently, the disposition of D10 complementarity-determining region loops is altered relative to that of most pMHCI-specific TCRs; the latter TCRs assume a diagonal orientation, although with substantial variability. Peptide recognition, which involves P-1 to P8 residues, is dominated by the Valpha domain, which also binds to the class II MHC beta1 helix. That docking is limited to one segment of MHC-bound peptide offers an explanation for epitope recognition and altered peptide ligand effects, suggests a structural basis for alloreactivity, and illustrates how bacterial superantigens can span the TCR-pMHCII surface.

PubMed: 10583947
DOI: 10.1126/science.286.5446.1913

Experimental method

X-RAY DIFFRACTION (3.2 Å)