1goz

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[[Image:1goz.gif|left|200px]]
[[Image:1goz.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1goz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1goz OCA], [http://www.ebi.ac.uk/pdbsum/1goz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1goz RCSB]</span>
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'''STRUCTURAL BASIS FOR THE ALTERED T-CELL RECEPTOR BINDING SPECIFICTY IN A SUPERANTIGENIC STAPHYLOCOCCUS AUREUS ENTEROTOXIN-B MUTANT'''
'''STRUCTURAL BASIS FOR THE ALTERED T-CELL RECEPTOR BINDING SPECIFICTY IN A SUPERANTIGENIC STAPHYLOCOCCUS AUREUS ENTEROTOXIN-B MUTANT'''
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[[Category: Baker, M D.]]
[[Category: Baker, M D.]]
[[Category: Papageorgiou, A C.]]
[[Category: Papageorgiou, A C.]]
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[[Category: enterotoxin b]]
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[[Category: Enterotoxin b]]
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[[Category: seb]]
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[[Category: Seb]]
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[[Category: staphylococcal enterotoxin]]
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[[Category: Staphylococcal enterotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:50:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:28 2008''
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Revision as of 14:50, 2 May 2008

Template:STRUCTURE 1goz

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 Page seeded by OCA on Fri May 2 17:50:21 2008

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