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Journal article

Crystal structure of a soluble CD28-Fab complex.

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...

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Publication status:
Published

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Publisher copy:
10.1038/ni1170

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Institution:
University of Oxford
Department:
Oxford, MSD, Experimental Medicine Division
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
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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

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