- Abstract:
-
Naive T cell activation requires signaling by the T cell receptor and by nonclonotypic cell surface receptors. The most important costimulatory protein is the monovalent homodimer CD28, which interacts with CD80 and CD86 expressed on antigen-presenting cells. Here we present the crystal structure of a soluble form of CD28 in complex with the Fab fragment of a mitogenic antibody. Structural comparisons redefine the evolutionary relationships of CD28-related proteins, antigen receptors and adhe...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1038/ni1170
-
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- Journal:
- Nature immunology
- Volume:
- 6
- Issue:
- 3
- Pages:
- 271-279
- Publication date:
- 2005-03-05
- DOI:
- EISSN:
-
1529-2916
- ISSN:
-
1529-2908
- URN:
-
uuid:5e25d640-30dd-4d52-bb72-c5d980fcc208
- Source identifiers:
-
23885
- Local pid:
- pubs:23885
- Copyright date:
- 2005
Journal article
Crystal structure of a soluble CD28-Fab complex.
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