1QLF

MHC CLASS I H-2DB COMPLEXED WITH GLYCOPEPTIDE K3G

Summary for 1QLF

• Entry DOI: 10.2210/pdb1qlf/pdb
• Descriptor: MHC CLASS I H-2DB HEAVY CHAIN, HUMAN BETA-2-MICROGLOBULIN, SYNTHETIC GLYCOPEPTIDE, ... (7 entities in total)
• Functional Keywords: immune system/peptide, murine class i mhc-peptide complex, mhc, glycopeptide, antigen, histocompatibility, immunology, immune system-peptide complex
• Biological source: MUS MUSCULUS (MOUSE); More
• Total number of polymer chains: 3
• Total formula weight: 45316.41

Authors

Tormo, J.,Jones, E.Y. (deposition date: 1999-08-30, release date: 1999-09-01, Last modification date: 2024-10-23)

Primary citation

Glithero, A.,Tormo, J.,Haurum, J.S.,Arsequell, G.,Valencia, G.,Edwards, J.,Springer, S.,Townsend, A.,Pao, Y.-L.,Wormald, M.,Dwek, R.A.,Jones, E.Y.,Elliot, T.
Crystal Structures of Two H-2Db/Glycopeptide Complexes Suggest a Molecular Basis for Ctl Cross-Reactivity
Immunity, 10:63-, 1999

PubMed Abstract: 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.

PubMed: 10023771
DOI: 10.1016/S1074-7613(00)80007-2

Experimental method

X-RAY DIFFRACTION (2.65 Å)