rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
4
|
pubmed:dateCreated |
1996-9-19
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR1 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Superantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin C, staphylococcal,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin F, Staphylococcal
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0022-2836
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
26
|
pubmed:volume |
260
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
553-69
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8759320-Amino Acid Sequence,
pubmed-meshheading:8759320-Bacterial Toxins,
pubmed-meshheading:8759320-Binding Sites,
pubmed-meshheading:8759320-Crystallography, X-Ray,
pubmed-meshheading:8759320-Enterotoxins,
pubmed-meshheading:8759320-HLA-DR1 Antigen,
pubmed-meshheading:8759320-Histocompatibility Antigens Class II,
pubmed-meshheading:8759320-Models, Molecular,
pubmed-meshheading:8759320-Molecular Sequence Data,
pubmed-meshheading:8759320-Protein Conformation,
pubmed-meshheading:8759320-Receptors, Antigen, T-Cell,
pubmed-meshheading:8759320-Sequence Homology, Amino Acid,
pubmed-meshheading:8759320-Staphylococcus aureus,
pubmed-meshheading:8759320-Superantigens,
pubmed-meshheading:8759320-Water
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pubmed:year |
1996
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pubmed:articleTitle |
The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 A resolution.
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pubmed:affiliation |
School of Biology and Biochemistry, University of Bath, Claverton Down, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|