1qlf: Difference between revisions
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|PDB= 1qlf |SIZE=350|CAPTION= <scene name='initialview01'>1qlf</scene>, resolution 2.65Å | |PDB= 1qlf |SIZE=350|CAPTION= <scene name='initialview01'>1qlf</scene>, resolution 2.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4 | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qlf OCA], [http://www.ebi.ac.uk/pdbsum/1qlf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qlf RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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== | ==About this Structure== | ||
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[[Category: Jones, E Y.]] | [[Category: Jones, E Y.]] | ||
[[Category: Tormo, J.]] | [[Category: Tormo, J.]] | ||
[[Category: antigen]] | [[Category: antigen]] | ||
[[Category: glycopeptide]] | [[Category: glycopeptide]] | ||
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[[Category: mhc]] | [[Category: mhc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:23 2008'' | ||