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Publication Abstract from PubMed
The pyrogenic toxin toxic shock syndrome toxin-1 from Staphylococcus aureus is a causative agent of the toxic shock syndrome disease. It belongs to a family of proteins known as superantigens that cross-link major histocompatibility class II molecules and T-cell receptors leading to the activation of a substantial number of T cells. The crystal structure of this protein has been refined to 2.07 A with an Rcryst value of 20.4% for 51,240 reflections. The final model contains three molecules in the asymmetric unit with good stereochemistry and a root-mean-square deviation of 0.009 A and 1.63 from ideality for bond lengths and bond angles, respectively. The overall fold is considerably similar to that of other known microbial superantigens (staphylococcal enterotoxins). However, a detailed structural analysis shows that toxic shock syndrome toxin-1 lacks several structural features that affect its specificity for V beta elements of the T-cell receptor and also its recognition by major histocompatibility class II molecules.
The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 A resolution.,Papageorgiou AC, Brehm RD, Leonidas DD, Tranter HS, Acharya KR J Mol Biol. 1996 Jul 26;260(4):553-69. PMID:8759320[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Papageorgiou AC, Brehm RD, Leonidas DD, Tranter HS, Acharya KR. The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 A resolution. J Mol Biol. 1996 Jul 26;260(4):553-69. PMID:8759320
