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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1988-6-22
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pubmed:abstractText |
The interactive association between T lymphocytes and their target cells is an important system of cell-cell interactions. Major histocompatibility complex class I molecules are the cell surface structures recognized by cytolytic T lymphocytes. To define the molecular structures recognized by cytotoxic T lymphocytes, we have saturated the 270-base-pair alpha 1 exon of the H-2Dp gene with point mutations, rapidly producing a "library" of 2.5 x 10(3) independent mutants. The library contains enough recombinant clones (each clone encoding approximately one amino acid replacement mutation) to predict a mutation at each nucleotide position of the alpha 1 exon. The functional analysis of the first five transfected gene products tested has shown that mutation of a conserved tyrosine at position 27 to asparagine destroys recognition of the H-2Dp gene product by polyclonal alloreactive cytotoxic T lymphocytes. Recognition of the same mutant molecule by three monoclonal antibodies and H-2-restricted lymphocytic choriomenengitis virus-specific cytotoxic T lymphocytes is unaffected.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-16589677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2413454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2420472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2426357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2432149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2433769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2434419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2439636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-2443855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3003746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3082989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3309677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3469146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3490919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3498790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3517656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3518748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3550437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3876513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-3964822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-4208792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-4399834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6095286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6184308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6184620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6196286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6205987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6209147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6260957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6323309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6961455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6978999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-6980415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3285344-92183
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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 |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3535-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3285344-Amino Acid Sequence,
pubmed-meshheading:3285344-Asparagine,
pubmed-meshheading:3285344-Base Sequence,
pubmed-meshheading:3285344-Cloning, Molecular,
pubmed-meshheading:3285344-Escherichia coli,
pubmed-meshheading:3285344-Genes, MHC Class I,
pubmed-meshheading:3285344-H-2 Antigens,
pubmed-meshheading:3285344-HLA Antigens,
pubmed-meshheading:3285344-Humans,
pubmed-meshheading:3285344-Models, Molecular,
pubmed-meshheading:3285344-Molecular Sequence Data,
pubmed-meshheading:3285344-Mutation,
pubmed-meshheading:3285344-Plasmids,
pubmed-meshheading:3285344-Protein Conformation,
pubmed-meshheading:3285344-T-Lymphocytes,
pubmed-meshheading:3285344-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:3285344-Tyrosine
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pubmed:year |
1988
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pubmed:articleTitle |
Saturation mutagenesis of a major histocompatibility complex protein domain: identification of a single conserved amino acid important for allorecognition.
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pubmed:affiliation |
Department of Microbiology and Immunology, University of North Carolina, Chapel Hill 27599.
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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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