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...
Main Authors: | Evans, E, Esnouf, R, Manso-Sancho, R, Gilbert, R, James, JR, Yu, C, Fennelly, J, Vowles, C, Hanke, T, Walse, B, Hünig, T, Sørensen, P, Stuart, D, Davis, S |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2005
|
Similar Items
-
The structure and cross-reactivity of CD28
by: Evans, E, et al.
Published: (2005) -
Topological requirements and signaling properties of T cell-activating, anti-CD28 antibody superagonists.
by: Lühder, F, et al.
Published: (2003) -
Crystallization of a soluble form of the rat T-cell surface glycoprotein CD4 complexed with Fab from the W3/25 monoclonal antibody.
by: Davis, S, et al.
Published: (1990) -
Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.
by: Jones, E, et al.
Published: (1992) -
CD28 co-stimulation in T-cell homeostasis: a recent perspective
by: Beyersdorf N, et al.
Published: (2015-05-01)