1goz
From Proteopedia
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| - | [[Image:1goz.gif|left|200px]] | + | [[Image:1goz.gif|left|200px]] |
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| - | '''STRUCTURAL BASIS FOR THE ALTERED T-CELL RECEPTOR BINDING SPECIFICTY IN A SUPERANTIGENIC STAPHYLOCOCCUS AUREUS ENTEROTOXIN-B MUTANT''' | + | {{Structure |
| + | |PDB= 1goz |SIZE=350|CAPTION= <scene name='initialview01'>1goz</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURAL BASIS FOR THE ALTERED T-CELL RECEPTOR BINDING SPECIFICTY IN A SUPERANTIGENIC STAPHYLOCOCCUS AUREUS ENTEROTOXIN-B MUTANT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GOZ is a [ | + | 1GOZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOZ OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and functional role of threonine 112 in a superantigen Staphylococcus aureus enterotoxin B., Baker MD, Papageorgiou AC, Titball RW, Miller J, White S, Lingard B, Lee JJ, Cavanagh D, Kehoe MA, Robinson JH, Acharya KR, J Biol Chem. 2002 Jan 25;277(4):2756-62. Epub 2001 Nov 9. PMID:[http:// | + | Structural and functional role of threonine 112 in a superantigen Staphylococcus aureus enterotoxin B., Baker MD, Papageorgiou AC, Titball RW, Miller J, White S, Lingard B, Lee JJ, Cavanagh D, Kehoe MA, Robinson JH, Acharya KR, J Biol Chem. 2002 Jan 25;277(4):2756-62. Epub 2001 Nov 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11704673 11704673] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: enterotoxin b]] | [[Category: enterotoxin b]] | ||
[[Category: seb]] | [[Category: seb]] | ||
| - | [[Category: staphylococcal | + | [[Category: staphylococcal enterotoxin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:26:00 2008'' |
Revision as of 09:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL BASIS FOR THE ALTERED T-CELL RECEPTOR BINDING SPECIFICTY IN A SUPERANTIGENIC STAPHYLOCOCCUS AUREUS ENTEROTOXIN-B MUTANT
Overview
Bacterial superantigens are potent T-cell stimulatory protein molecules produced by Staphylococcus aureus and Streptococcus pyogenes. Their superantigenic activity can be attributed to their ability to cross-link major histocompatibility complex class II molecules with T-cell receptors (TCRs) to form a tri-molecular complex. Each superantigen is known to interact with a specific V(beta) element of TCR. Staphylococcal enterotoxin B (SEB, a superantigen), a primary cause of food poisoning, is also responsible for a significant percentage of non-menstrual associated toxic shock syndrome in patients with a variety of staphylococcal infections. Structural studies have elucidated a binding cavity on the toxin molecule essential for TCR binding. To understand the crucial residues involved in binding, mutagenesis analysis was performed. Our analysis suggest that mutation of a conserved residue Thr(112) to Ser (T112S) in the binding cavity induces a selective reduction in the affinity for binding one TCR V(beta) family and can be attributed to the structural differences in the native and mutant toxins. We present a detailed comparison of the mutant structure determined at 2.0 A with the previously reported native SEB and SEB-TCR V(beta) complex structures.
About this Structure
1GOZ is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structural and functional role of threonine 112 in a superantigen Staphylococcus aureus enterotoxin B., Baker MD, Papageorgiou AC, Titball RW, Miller J, White S, Lingard B, Lee JJ, Cavanagh D, Kehoe MA, Robinson JH, Acharya KR, J Biol Chem. 2002 Jan 25;277(4):2756-62. Epub 2001 Nov 9. PMID:11704673
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