Dec 3, 1999

The crystal structure of a T cell receptor in complex with peptide and MHC class II

Science
E L ReinherzJ Wang

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.

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Mentioned in this Paper

Human Class I Antigens
Molecular Helix
Conalbumin
Suppressor T-Lymphocytes, CD8-Positive
Tertiary Protein Structure
Helix (Snails)
Oligopeptides
Crystallography, X-Ray
Genes, MHC Class II
Docking -molecular Interaction

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