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rdf:type |
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lifeskim:mentions |
umls-concept:C0019630,
umls-concept:C0038402,
umls-concept:C0205314,
umls-concept:C0206527,
umls-concept:C0376525,
umls-concept:C0444626,
umls-concept:C0679622,
umls-concept:C1148621,
umls-concept:C1513371,
umls-concept:C1704675,
umls-concept:C1705535
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pubmed:issue |
8
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pubmed:dateCreated |
1997-9-4
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pubmed:abstractText |
Bacterial superantigens are small proteins that have a very potent stimulatory effect on T lymphocytes through their ability to bind to both MHC class II molecules and T-cell receptors. We have determined the three-dimensional structure of a Streptococcal superantigen, SPE-C, at 2.4 A resolution. The structure shows that SPE-C has the usual superantigen fold, but that the surface that forms a generic, low-affinity MHC-binding site in other superantigens is here used to create a SPE-C dimer. Instead, MHC class II binding occurs through a zinc binding site that is analogous to a similar site in staphylococcal enterotoxin A. Consideration of the SPE-C dimer suggests a novel mechanism for promotion of MHC aggregation and T-cell activation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Exotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/SpeA protein, Streptococcus pyogenes,
http://linkedlifedata.com/resource/pubmed/chemical/Superantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin F, Staphylococcal,
http://linkedlifedata.com/resource/pubmed/chemical/erythrogenic toxin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
635-43
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9253413-Amino Acid Sequence,
pubmed-meshheading:9253413-Antigens, Bacterial,
pubmed-meshheading:9253413-Bacterial Proteins,
pubmed-meshheading:9253413-Bacterial Toxins,
pubmed-meshheading:9253413-Binding Sites,
pubmed-meshheading:9253413-Computer Simulation,
pubmed-meshheading:9253413-Crystallography, X-Ray,
pubmed-meshheading:9253413-Dimerization,
pubmed-meshheading:9253413-Enterotoxins,
pubmed-meshheading:9253413-Exotoxins,
pubmed-meshheading:9253413-Histocompatibility Antigens Class II,
pubmed-meshheading:9253413-Lymphocyte Activation,
pubmed-meshheading:9253413-Membrane Proteins,
pubmed-meshheading:9253413-Models, Biological,
pubmed-meshheading:9253413-Models, Molecular,
pubmed-meshheading:9253413-Molecular Sequence Data,
pubmed-meshheading:9253413-Receptors, Antigen, T-Cell,
pubmed-meshheading:9253413-Sequence Homology, Amino Acid,
pubmed-meshheading:9253413-Streptococcus pyogenes,
pubmed-meshheading:9253413-Superantigens,
pubmed-meshheading:9253413-T-Lymphocytes,
pubmed-meshheading:9253413-Zinc
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pubmed:year |
1997
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pubmed:articleTitle |
Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules.
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pubmed:affiliation |
Department of Biochemistry, Massey University, Palmerston North, New Zealand.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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