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Crystal structure of a soluble CD28-Fab complex
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Evans, Edward J, Esnouf, Robert M, Manso-Sancho, Raquel, Gilbert, Robert J C, James, John R., Yu, Chao, Fennelly, Janet A, Vowles, Cheryl, Hanke, Thomas, Walse, Björn, Hünig, Thomas, Sørensen, Poul, Stuart, David I and Davis, Simon J (2005) Crystal structure of a soluble CD28-Fab complex. Nature Immunology, 6 (3). pp. 271-279. doi:10.1038/ni1170 ISSN 1529-2908.
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Official URL: http://dx.doi.org/10.1038/ni1170
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 adhesion molecules and account for the distinct ligand-binding and stoichiometric properties of CD28 and the related, inhibitory homodimer CTLA-4. Cryo-electron microscopy-based comparisons of complexes of CD28 with mitogenic and nonmitogenic antibodies place new constraints on models of antibody-induced receptor triggering. This work completes the initial structural characterization of the CD28-CTLA-4-CD80-CD86 signaling system.
Item Type: | Journal Article | ||||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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Journal or Publication Title: | Nature Immunology | ||||||||
Publisher: | Nature Publishing Group | ||||||||
ISSN: | 1529-2908 | ||||||||
Official Date: | March 2005 | ||||||||
Dates: |
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Volume: | 6 | ||||||||
Number: | 3 | ||||||||
Page Range: | pp. 271-279 | ||||||||
DOI: | 10.1038/ni1170 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access |
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