1ce6

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==Overview==
==Overview==
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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.
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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==
==Disease==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
[[Category: Tormo, J.]]
[[Category: Tormo, J.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: viral peptide]]
[[Category: viral peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:35:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:10 2008''

Revision as of 10:05, 21 February 2008


1ce6, resolution 2.90Å

Drag the structure with the mouse to rotate

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

Contents

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

1CE6 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with as ligand. 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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