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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1998-7-21
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pubmed:abstractText |
A synthetic tridecapeptide, corresponding to the 30-42 fragment of the S1 subunit of pertussis toxin, has been structurally characterised by using NMR spectroscopy. The molecule corresponds to a T-cell epitope of the bacterial toxin which has been extensively analysed with the alanine scanning approach to check the relevance of each residue for the biological activity of the peptide. Five of these Ala-substituted analogs have also been spectroscopically studied. In the experimental conditions used, different extents of helicity were found for the six peptides in a way which cannot be related to their capabilities of of binding to major histocompatibility complex (MHC) class II and inducing T-cell proliferation. Backbone flexibility around helical transient conformations seems to constitute the structural intermediate step between the structure of the corresponding sequence within the parental protein and in the MHC class II complex. A model of the latter complex, which accounts for the different biological activities of the analogs, is proposed.
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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/Epitopes, T-Lymphocyte,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinin Glycoproteins...,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Vaccines, Synthetic,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
254
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
313-7
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:9660185-Amino Acid Sequence,
pubmed-meshheading:9660185-Drug Design,
pubmed-meshheading:9660185-Epitopes, T-Lymphocyte,
pubmed-meshheading:9660185-Hemagglutinin Glycoproteins, Influenza Virus,
pubmed-meshheading:9660185-Histocompatibility Antigens Class II,
pubmed-meshheading:9660185-Humans,
pubmed-meshheading:9660185-Macromolecular Substances,
pubmed-meshheading:9660185-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9660185-Models, Molecular,
pubmed-meshheading:9660185-Peptide Fragments,
pubmed-meshheading:9660185-Pertussis Toxin,
pubmed-meshheading:9660185-Protein Conformation,
pubmed-meshheading:9660185-Protein Structure, Secondary,
pubmed-meshheading:9660185-Structure-Activity Relationship,
pubmed-meshheading:9660185-Vaccines, Synthetic,
pubmed-meshheading:9660185-Virulence Factors, Bordetella
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pubmed:year |
1998
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pubmed:articleTitle |
NMR studies on the structure/function correlations of T-cell-epitope analogs from pertussis toxin.
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pubmed:affiliation |
Biomolecular Structure Research Center and Dipartimento di Biologia Molecolare, University of Siena, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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