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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6394
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pubmed:dateCreated |
1992-11-16
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pubmed:abstractText |
T cells recognize foreign protein antigens in the form of peptide fragments bound tightly to the outer aspect of molecules encoded by the major histocompatibility complex (MHC). Most of the amino-acid differences that distinguish MHC allelic variants line the peptide-binding cleft, and different allelic forms of MHC molecules bind distinct peptides. It has been demonstrated that peptide-binding to MHC class I involves anchor residues in certain positions and that antigenic peptides associated with MHC class I exhibit allele-specific structural motifs. We have previously reported an analysis of MHC class II-associated peptide sequences. Here we extend this analysis and show that certain amino-acid residues occur at particular positions in the sequence of peptides binding to a given MHC class II molecule. These sequence motifs require the amino terminus to be shifted one or two positions to obtain alignment; such shifts occur naturally for a single peptide sequence without qualitatively altering CD4 T-cell recognition.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/I-E-antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Variable Region,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/methionine repressor protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0028-0836
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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 |
359
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
429-31
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:1328884-Amino Acid Sequence,
pubmed-meshheading:1328884-Animals,
pubmed-meshheading:1328884-Antigen-Antibody Reactions,
pubmed-meshheading:1328884-Bacterial Proteins,
pubmed-meshheading:1328884-Binding Sites, Antibody,
pubmed-meshheading:1328884-Cell Line,
pubmed-meshheading:1328884-Chromatography, High Pressure Liquid,
pubmed-meshheading:1328884-Histocompatibility Antigens Class II,
pubmed-meshheading:1328884-Immunoglobulin G,
pubmed-meshheading:1328884-Immunoglobulin Heavy Chains,
pubmed-meshheading:1328884-Immunoglobulin Variable Region,
pubmed-meshheading:1328884-Mice,
pubmed-meshheading:1328884-Mice, Inbred C57BL,
pubmed-meshheading:1328884-Molecular Sequence Data,
pubmed-meshheading:1328884-Peptide Fragments,
pubmed-meshheading:1328884-Receptors, Transferrin,
pubmed-meshheading:1328884-Repressor Proteins,
pubmed-meshheading:1328884-Sequence Alignment,
pubmed-meshheading:1328884-Sequence Homology, Amino Acid,
pubmed-meshheading:1328884-T-Lymphocytes,
pubmed-meshheading:1328884-Viral Envelope Proteins
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pubmed:year |
1992
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pubmed:articleTitle |
Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs.
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pubmed:affiliation |
ImmuLogic Pharmaceutical Corporation, Palo Alto, California 94304.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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