1qlf

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spinqualitylabelsall models 1qlf, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MHC CLASS I H-2DB COMPLEXED WITH GLYCOPEPTIDE K3G

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Two synthetic O-GlcNAc-bearing peptides that elicit H-2Db-restricted, glycopeptide-specific cytotoxic T cells (CTL) have been shown to display, nonreciprocal patterns of cross-reactivity. Here, we present the crystal, structures of the H-2Db glycopeptide complexes to 2.85 A resolution or, better. In both cases, the glycan is solvent exposed and available for, direct recognition by the T cell receptor (TCR). We have modeled the, complex formed between the MHC-glycopeptide complexes and their respective, TCRs, showing that a single saccharide residue can be accommodated in the, standard TCR-MHC geometry. The models also reveal a possible molecular, basis for the observed cross-reactivity patterns of the CTL clones, which, appear to be influenced by the length of the CDR3 loop and the nature of, the immunizing ligand.

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

1QLF is a Protein complex structure of sequences from Homo sapiens, Mus musculus and Sendai virus with NAG, SO4 and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity., Glithero A, Tormo J, Haurum JS, Arsequell G, Valencia G, Edwards J, Springer S, Townsend A, Pao YL, Wormald M, Dwek RA, Jones EY, Elliott T, Immunity. 1999 Jan;10(1):63-74. PMID:10023771

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