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1qlf
From Proteopedia
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| , resolution 2.65Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MHC CLASS I H-2DB COMPLEXED WITH GLYCOPEPTIDE K3G
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.
About this Structure
1QLF is a Protein complex structure of sequences from Homo sapiens, Mus musculus and Sendai virus. 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
Page seeded by OCA on Sun Mar 30 23:15:23 2008
