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Pubmed ID :15696168
Publication Date : 2005/02/17

Crystal structure of a soluble CD28-Fab complex.


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.

Authors : 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 , Davis Simon J ,

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