rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
2
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pubmed:dateCreated |
1997-7-14
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pubmed:abstractText |
Staphylococcal enterotoxins and toxic shock syndrome toxin-1 are known as superantigens due to their ability to activate a large number of T-cells by crosslinking the major histocompatibility complex class II molecules with the T-cell receptor. Although superantigens seem to act by a common mechanism, they vary in many of their specific interactions and biological properties. A structural comparison of staphylococcal enterotoxins A and C2, members of the staphylococcal superantigens, has shown large conformational differences at the putative TcR interaction site (loops between alphaN-alpha2, alpha4-beta9 and beta10-alpha5 in staphylococcal enterotoxin A) that could explain the variability in their T-cell receptor specificity. A common Zn2(+)-binding site was identified in both staphylococcal enterotoxin A and C2 that is superimposable but differs somewhat in its coordination geometry between the two 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/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR1 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Superantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin A, Staphylococcal,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin C, staphylococcal
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-2836
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
270-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9191070-Amino Acid Sequence,
pubmed-meshheading:9191070-Antigens, Bacterial,
pubmed-meshheading:9191070-Binding Sites,
pubmed-meshheading:9191070-Enterotoxins,
pubmed-meshheading:9191070-HLA-DR1 Antigen,
pubmed-meshheading:9191070-Models, Molecular,
pubmed-meshheading:9191070-Molecular Sequence Data,
pubmed-meshheading:9191070-Protein Binding,
pubmed-meshheading:9191070-Protein Conformation,
pubmed-meshheading:9191070-Receptors, Antigen, T-Cell,
pubmed-meshheading:9191070-Sequence Alignment,
pubmed-meshheading:9191070-Sequence Homology, Amino Acid,
pubmed-meshheading:9191070-Superantigens,
pubmed-meshheading:9191070-Zinc
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pubmed:year |
1997
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pubmed:articleTitle |
A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity.
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pubmed:affiliation |
Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Lund University, Sweden.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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