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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1987-11-9
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pubmed:databankReference | |
pubmed:abstractText |
The murine equivalent of the cDNA encoding the human T11 (CD2) sheep erythrocyte-binding protein has been cloned. It codes for a putative transmembrane protein which is homologous to human T11. In contrast to immunoglobulins whose domains consist of anti-parallel beta sheets, we predict that mouse and human T11 external domains probably belong to the alpha/beta protein folding class. The cytoplasmic region of T11 is a lengthy, proline-rich segment; secondary structural analysis predicts it to have a nonglobular conformation. This elongated tail could allow for interaction with multiple other intracellular proteins and may contain a cation-binding site involved in T lineage activation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-2980
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1367-70
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2820751-Amino Acid Sequence,
pubmed-meshheading:2820751-Animals,
pubmed-meshheading:2820751-Antigens, CD27,
pubmed-meshheading:2820751-Antigens, Surface,
pubmed-meshheading:2820751-Base Sequence,
pubmed-meshheading:2820751-DNA,
pubmed-meshheading:2820751-Genes,
pubmed-meshheading:2820751-Humans,
pubmed-meshheading:2820751-Mice,
pubmed-meshheading:2820751-Molecular Sequence Data,
pubmed-meshheading:2820751-Protein Conformation
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pubmed:year |
1987
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pubmed:articleTitle |
Murine and human T11 (CD2) cDNA sequences suggest a common signal transduction mechanism.
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pubmed:affiliation |
Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA 02115.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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