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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6398
|
pubmed:dateCreated |
1992-12-1
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pubmed:abstractText |
The three-dimensional structure of staphylococcal enterotoxin B, which is both a toxin and a super-antigen, has been determined to a resolution of 2.5 A. The unusual main-chain fold containing two domains may represent a general motif adopted by all staphylococcal enterotoxins. The T-cell receptor binding site encompasses a shallow cavity formed by both domains. The MHCII molecule binds to an adjacent site. Another cavity with possible biological activity was also identified.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
29
|
pubmed:volume |
359
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
801-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1436058-Animals,
pubmed-meshheading:1436058-Antigens, Bacterial,
pubmed-meshheading:1436058-Binding Sites,
pubmed-meshheading:1436058-Enterotoxins,
pubmed-meshheading:1436058-Models, Molecular,
pubmed-meshheading:1436058-Protein Conformation,
pubmed-meshheading:1436058-Protein Structure, Secondary,
pubmed-meshheading:1436058-Receptors, Antigen, T-Cell,
pubmed-meshheading:1436058-Staphylococcus aureus,
pubmed-meshheading:1436058-X-Ray Diffraction
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pubmed:year |
1992
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pubmed:articleTitle |
Crystal structure of staphylococcal enterotoxin B, a superantigen.
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pubmed:affiliation |
Biocrystallography Laboratory, VA Medical Center, Pittsburgh, Pennsylvania 15240.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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