|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0017355,
umls-concept:C0024518,
umls-concept:C0085358,
umls-concept:C0127400,
umls-concept:C0205148,
umls-concept:C0337611,
umls-concept:C0439064,
umls-concept:C0456387,
umls-concept:C1332717,
umls-concept:C1413244,
umls-concept:C1514562,
umls-concept:C1552866,
umls-concept:C1704675,
umls-concept:C1706438,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1979845,
umls-concept:C2003941,
umls-concept:C2698600,
umls-concept:C2700399
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1995-12-4
|
|
pubmed:abstractText |
The cell surface glycoprotein CD8 functions as a coreceptor with the TCR on cytotoxic T lymphocytes. Mutational analysis of the binding site of CD8 for MHC class I predicted that distinct surfaces of CD8 would interact with both the alpha 2 and alpha 3 domains of class I. Using a cell-cell adhesion assay, we identified three residues Q115, D122, and E128 in the alpha 2 domain of class I critical for interaction with CD8. The side chains of these residues point towards a cavity formed by the alpha 1/alpha 2 platform, the alpha 3 domain and beta 2-microglobulin (beta 2m) of class I. These residues were predicted to contact CD8 based on a bivalent model of interaction between one CD8 alpha/alpha homodimer and two MHC class I molecules. These results therefore provide support for the model.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-1350981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-1374450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-1439792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-15336032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-1547508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-1652099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-1906921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-1908563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2038058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2109837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2437024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2443855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2459215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2475477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2784196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-2955903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-3031507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-3032784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-3263576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-3819393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-3881765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-6167544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-6604917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-7529940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-7824949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-7830771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-7913109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-8001128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-8043041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-8127870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-8296156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-8316295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7595198-8347296
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0022-1007
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
182
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1275-80
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:7595198-Animals,
pubmed-meshheading:7595198-Antigens, CD8,
pubmed-meshheading:7595198-Binding Sites,
pubmed-meshheading:7595198-CHO Cells,
pubmed-meshheading:7595198-Cell Adhesion,
pubmed-meshheading:7595198-Cell Line,
pubmed-meshheading:7595198-Cercopithecus aethiops,
pubmed-meshheading:7595198-Cricetinae,
pubmed-meshheading:7595198-DNA, Complementary,
pubmed-meshheading:7595198-HLA-A2 Antigen,
pubmed-meshheading:7595198-Models, Molecular,
pubmed-meshheading:7595198-Mutagenesis, Site-Directed,
pubmed-meshheading:7595198-Protein Binding,
pubmed-meshheading:7595198-Protein Conformation,
pubmed-meshheading:7595198-beta 2-Microglobulin
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the alpha 2 and alpha 3 domains of MHC class I.
|
|
pubmed:affiliation |
Department of Laboratory Medicine, Yale University School of Medicine, New Haven, Connecticut 06520-8035, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
