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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-2-15
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pubmed:abstractText |
Staphylococcal enterotoxins (SEs) are superantigenic protein toxins responsible for a number of life-threatening diseases. The X-ray structure of a staphylococcal enterotoxin A (SEA) triple-mutant (L48R, D70R, and Y92A) vaccine reveals a cascade of structural rearrangements located in three loop regions essential for binding the alpha subunit of major histocompatibility complex class II (MHC-II) molecules. A comparison of hypothetical model complexes between SEA and the SEA triple mutant with MHC-II HLA-DR1 clearly shows disruption of key ionic and hydrophobic interactions necessary for forming the complex. Extensive dislocation of the disulfide loop in particular interferes with MHC-IIalpha binding. The triple-mutant structure provides new insights into the loss of superantigenicity and toxicity of an engineered superantigen and provides a basis for further design of enterotoxin vaccines.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-10066883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-10479175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-10850798,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-11163233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-13990617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-1509257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-1832875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-2185544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-2377208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-2401011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-6667333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7506550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7542584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7595227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7628431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7648392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7650479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7664123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7822779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-7997880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8152483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8225606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8486972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8538573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8618863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8662544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8692262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8699064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8892628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8906788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-8906797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-9217771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-9254694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-9500785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-9795392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11847286-9881971
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
642-51
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11847286-Amino Acid Substitution,
pubmed-meshheading:11847286-Cell Line,
pubmed-meshheading:11847286-Enterotoxins,
pubmed-meshheading:11847286-Genes, MHC Class II,
pubmed-meshheading:11847286-Histocompatibility Antigens Class II,
pubmed-meshheading:11847286-Humans,
pubmed-meshheading:11847286-Models, Molecular,
pubmed-meshheading:11847286-Mutation,
pubmed-meshheading:11847286-Protein Binding,
pubmed-meshheading:11847286-Protein Conformation,
pubmed-meshheading:11847286-Protein Structure, Tertiary,
pubmed-meshheading:11847286-Sequence Homology,
pubmed-meshheading:11847286-Staphylococcal Vaccines,
pubmed-meshheading:11847286-Structure-Activity Relationship,
pubmed-meshheading:11847286-Superantigens
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pubmed:year |
2002
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pubmed:articleTitle |
Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC-IIalpha.
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pubmed:affiliation |
Lawrence Livermore National Laboratory, Macromolecular Crystallography, Biology and Biotechnology Research Program, University of California, Livermore, California 94551, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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