1CE6

MHC CLASS I H-2DB COMPLEXED WITH A SENDAI VIRUS NUCLEOPROTEIN PEPTIDE

Summary for 1CE6

• Entry DOI: 10.2210/pdb1ce6/pdb
• Descriptor: PROTEIN (MHC CLASS I H-2DB HEAVY CHAIN), PROTEIN (HUMAN BETA-2 MICROGLOBULIN), PROTEIN (SENDAI VIRUS NUCLEOPROTEIN), ... (5 entities in total)
• Functional Keywords: mhc class i, antigen presentation, viral peptide, complex
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01899; Secreted: P61769; Virion (Potential): P04858
• Total number of polymer chains: 3
• Total formula weight: 45762.00

Authors

Tormo, J.,Jones, E.Y. (deposition date: 1999-03-17, release date: 1999-03-26, Last modification date: 2024-11-20)

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.,Elliott, T.
Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity.
Immunity, 10:63-74, 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 (2.9 Å)