1goz
From Proteopedia
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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 Tue Nov 20 16:12:44 2007
