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The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 A resolution.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Papageorgiou AC,Brehm RD,Leonidas DD,Tranter HS,Acharya KR

doi

10.1006/jmbi.1996.0421

subject

Has Abstract

pub_date

1996-07-26 00:00:00

pages

553-69

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022283696904210

journal_volume

260

pub_type

杂志文章

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