rdf:type |
|
lifeskim:mentions |
umls-concept:C0034790,
umls-concept:C0085379,
umls-concept:C0086418,
umls-concept:C0108779,
umls-concept:C0302350,
umls-concept:C0439098,
umls-concept:C0439855,
umls-concept:C0444626,
umls-concept:C1552644,
umls-concept:C1823153,
umls-concept:C2349976
|
pubmed:issue |
20
|
pubmed:dateCreated |
2004-5-19
|
pubmed:databankReference |
|
pubmed:abstractText |
The CD3 epsilon gamma heterodimer is essential for expression and function of the T cell receptor. The crystal structure of the human CD3 epsilon gamma heterodimer is described to 2.1-A resolution complexed with OKT3, a therapeutic mAb that not only activates and tolerizes mature T cells but also induces regulatory T cells. The mode of CD3 epsilon gamma dimerization provides a general structural basis for CD3 assembly and maps candidate T cell antigen receptor docking sites, including a duplicated linear region rich in acidic residues that is unique to human CD3 epsilon. OKT3 binds to an atypically small area of CD3 epsilon and has a low affinity for the isolated CD3 epsilon gamma heterodimer. The structure of the OKT3/CD3 epsilon gamma complex has implications for T cell signaling and therapeutic design.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15136729-10146352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15136729-10398592,
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|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0027-8424
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
18
|
pubmed:volume |
101
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
7675-80
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:15136729-Amino Acid Sequence,
pubmed-meshheading:15136729-Animals,
pubmed-meshheading:15136729-Antigens, CD3,
pubmed-meshheading:15136729-Crystallization,
pubmed-meshheading:15136729-Dimerization,
pubmed-meshheading:15136729-Humans,
pubmed-meshheading:15136729-Mice,
pubmed-meshheading:15136729-Molecular Sequence Data,
pubmed-meshheading:15136729-Muromonab-CD3,
pubmed-meshheading:15136729-Protein Binding,
pubmed-meshheading:15136729-Protein Structure, Tertiary,
pubmed-meshheading:15136729-Surface Plasmon Resonance
|
pubmed:year |
2004
|
pubmed:articleTitle |
Crystal structure of the human T cell receptor CD3 epsilon gamma heterodimer complexed to the therapeutic mAb OKT3.
|
pubmed:affiliation |
Department of Microbiology and Immunology, University of Melbourne, Parkville, Victoria 3010, Australia.
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pubmed:publicationType |
Journal Article
|